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L3 ANSWER 1 OF 46 CA COPYRIGHT 1996 ACS
AN 124:197662 CA
TI Simple force field for study of peptide and protein conformational
properties
AU Creamer, Trevor P.; ***Rose, George D.***
CS School Medicine, Johns Hopkins University, Baltimore, MD, 21205, USA
SO Methods Enzymol. (1995), 259(Energetics of Biological
Macromolecules), 576-89
CODEN: MENZAU; ISSN: 0076-6879
DT Journal
LA English
CC 9-16 (Biochemical Methods)
Section cross-reference(s): 6
AB CRASS, a simple force field for use in the study of conformational
properties of peptides and proteins, has been derived.
ST force field peptide protein conformation
IT Conformation and Conformers
(simple force field for study of peptide and protein
conformational properties)
IT Peptides, properties
Proteins, properties
RL: PRP (Properties)
(simple force field for study of peptide and protein
conformational properties)
L3 ANSWER 2 OF 46 CA COPYRIGHT 1996 ACS
AN 124:24288 CA
TI Modeling unfolded states of peptides and proteins
AU Creamer, Trevor P.; Srinivasan, Rajgopal; ***Rose, George D.***
CS School of Medicine, Johns Hopkins University, Baltimore, MD, 21205,
USA
SO Biochemistry (1995), 34(50), 16245-50
CODEN: BICHAW; ISSN: 0006-2960
DT Journal
LA English
CC 6-3 (General Biochemistry)
Section cross-reference(s): 9
OS CJACS-IMAGE; CJACS
AB The hydrophobic effect is the major factor that drives a protein
mol. toward collapse and folding. In this process, residues with
apolar side chains assoc. to form a solvent-shielded hydrophobic
core. Often, this hydrophobic contribution to folding is quantified
by measuring buried apolar surface area, reckoned as the difference
in area between hydrophobic groups in the folded protein and in a
std. state. Typically, the std. state area of a residue is obtained
from tripeptide models, with the results taken to implicitly
represent values appropriate for the unfolded state. Here, the
authors show that a tripeptide is a poor descriptor of the unfolded
state, and its widespread use has prompted erroneous conclusions
about folding. As an alternative, the authors explore two limiting
models, chosen to bracket the expected behavior of the unfolded
chain between reliable extremes. One extreme is represented by
simulated hard-sphere peptides and shown to behave like a
homopolymer with excluded vol. in a good solvent. The other extreme
is represented by fragments excised from folded proteins and
conjectured to approx. the time-av. behavior of a thermally
denatured protein at Tm, the midpoint of the unfolding transition.
Using these models, it is shown that the area buried by apolar side
chains upon folding is considerably less than earlier ests. For
example, upon transfer from the unfolded state to the middle of an
.alpha.-helix, an alanine side chain buries negligible area and,
surprisingly, a valine side chain actually gains area. Among other
applications, an improved model of the unfolded state can be used to
better evaluate the driving force for helix formation in peptides
and proteins.
ST model peptide protein unfolding
IT Conformation and Conformers
(folding; modeling unfolded states of peptides and proteins)
IT Molecular modeling
Simulation and Modeling, physicochemical
(modeling unfolded states of peptides and proteins)
IT Peptides, properties
Proteins, properties
RL: PEP (Physical, engineering or chemical process); PRP
(Properties); PROC (Process)
(modeling unfolded states of peptides and proteins)
IT 52-90-4, Cysteine, properties 56-40-6, Glycine, properties
56-41-7, Alanine, properties 56-45-1, Serine, properties
56-84-8, Aspartic acid, properties 56-85-9, Glutamine, properties
56-86-0, Glutamic acid, properties 56-87-1, Lysine, properties
60-18-4, Tyrosine, properties 61-90-5, Leucine, properties
63-68-3, Methionine, properties 63-91-2, (Phenylalanine),
properties 70-47-3, Asparagine, properties 71-00-1, (Histidine),
properties 72-18-4, Valine, properties 72-19-5, Threonine,
properties 73-22-3, Tryptophan, properties 73-32-5, Isoleucine,
properties 74-79-3, Arginine, properties 147-85-3, Proline,
properties
RL: PRP (Properties)
(modeling unfolded states of peptides and proteins)
L3 ANSWER 3 OF 46 CA COPYRIGHT 1996 ACS
AN 123:250588 CA
TI Rigid domains in proteins: an algorithmic approach to their
identification
AU Nichols, William L.; ***Rose, George D.*** ; Eyck, Lynn F. Ten;
Zimm, Bruno H.
CS Dep. of cheimstry and Biochemistry, Univ. of California, San Diego,
CA, 92093, USA
SO Proteins: Struct., Funct., Genet. (1995), 23(1), 38-48
CODEN: PSFGEY; ISSN: 0887-3585
DT Journal
LA English
CC 9-16 (Biochemical Methods)
AB A rigid domain, defined here as a tertiary structure common to two
or more different protein conformations, can be identified
numerically from at. coordinates by finding sets of residues, one in
each conformation, such that th distance between any two residues
within the set belonging to one conformation is the same as the
distance between the two structurally equiv. residues within the set
belonging to any other conformation. The distance between two
residues is taken to the distance between their resp. .alpha. carbon
atoms. With the methods of this paper we have found in the deoxy
and oxy conformations of the human Hb .alpha.1.beta.1 dimer a rigid
domain closely related to that previously identified by Baldwin and
Chothia (J. Mol. Biol. 129: 175-220, 1979). We provide two
algorithms, both using the difference-distance matrix, with which to
search for rigid domains directly from at. coordinates. The first
finds all rigid domains in a protein but has storage and processing
demands that become prohibitively large with increasing protein
size. The second, although not necessarily finding every rigid
domain, is computationally tractable for proteins of any size.
Because of its efficiency we are able to search protein
conformations recursively for groups of non-intersecting domains.
Different protein conformations, when aligned by superimposing their
resp. domain structures, can be examd. for structural differences in
regions complementing a rigid domain.
ST protein conformation rigid domain algorithmic approach
IT Conformation and Conformers
(an algorithmic approach to their identification of rigid domains
in proteins)
IT Proteins, properties
RL: PRP (Properties)
(an algorithmic approach to their identification of rigid domains
in proteins)
L3 ANSWER 4 OF 46 CA COPYRIGHT 1996 ACS
AN 123:78968 CA
TI LINUS: A hierarchic procedure to predict the fold of a protein
AU Srinivasan, Rajgopal; ***Rose, George D.***
CS Department of Biophysics and Biophysical Chemistry, Johns Hopkins
University School of Medicine, Baltimore, MD, 21205, USA
SO Proteins: Struct., Funct., Genet. (1995), 22(2), 81-99
CODEN: PSFGEY; ISSN: 0887-3585
DT Journal
LA English
CC 9-16 (Biochemical Methods)
Section cross-reference(s): 6
AB The authors describe LINUS, a hierarchic procedure to predict the
fold of a protein from its amino acid sequence alone. The
algorithm, which has been implemented in a computer program, was
applied to large, overlapping fragments from a diverse test set of 7
x-ray-elucidated proteins, with encouraging results. For all
proteins but one, the overall fragment topol. is well predicted,
including both secondary and supersecondary structure. The
algorithm was also applied to a mol. of unknown conformation, groES,
in which x-ray structure detn. is presently ongoing. LINUS is an
acronym for Local Independently Nucleated Units of STructure. The
procedure ascends the folding hiearchy in discrete stages, with
concomitant accretion of structure at each step. The chain is
represented by simplified geometry and folds under the influence of
a primitive energy function. The only accurately described
energetic quantity in this work is hard sphere repulsion-the
principal force involved in organizing protein conformation
[Richards, F. M. Ann. Rev. Biophys. Bioeng. 6:151-176, 1977]. Among
other applications, the method is a natural tool for use in the
human genome initiative.
ST LINUS hierarchic predict fold protein
IT Algorithm
Conformation and Conformers
Genome
Protein sequences
(LINUS: A hierarchic procedure to predict the fold of a protein)
IT Proteins, properties
RL: PRP (Properties)
(LINUS: A hierarchic procedure to predict the fold of a protein)
L3 ANSWER 5 OF 46 CA COPYRIGHT 1996 ACS
AN 123:77560 CA
TI Interactions between hydrophobic side chains within .alpha.-helixes
AU Creamer, Trevor P.; ***Rose, George D.***
CS Dep. Biophysics Biophysical Chemistry, Johns Hopkins Univ. School
Medicine, Baltimore, MD, 21205, USA
SO Protein Sci. (1995), 4(7), 1305-14
CODEN: PRCIEI; ISSN: 0961-8368
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB The thermodn. basis of helix stability in peptides and proteins is a
topic of considerable interest. Accordingly, the authors computed
the interactions between side-chains of all hydrophobic residue
pairs and selected triples in a model helix, using
Boltzmann-weighted exhaustive modeling. Specifically, all possible
pairs from the set, Ala, Cys, His, Ile, Leu, Met, Phe, Trp, Tyr, and
Val, were modeled at spacings of (i, i+2), (i, i+3), and (i, i+4) in
the central turn of a model polyalanyl .alpha.-helix. Significant
interactions, both stabilizing and destabilizing, were found to
occur at spacings of (i, i+3) and (i, i+4), particularly in
side-chains with rings (i.e., Phe, Tyr, Trp, and His). In addn.,
modeling of Leu triples in a helix showed that the free energy could
exceed the sum of pairwise interactions in certain cases. The
calcd. interaction values both rationalized recent exptl. data and
provided previously unavailable ests. of the constituent energies
and entropies of interaction.
ST alpha helix stability peptide protein thermodn
IT Peptides, biological studies
Proteins, biological studies
RL: BPR (Biological process); PRP (Properties); BIOL (Biological
study); PROC (Process)
(interactions between hydrophobic side-chains within
.alpha.-helixes of peptides and proteins)
IT Thermodynamics
(thermodn. basis of .alpha.-helix stability in proteins and
peptides)
IT Conformation and Conformers
(.alpha.-helical, interactions between hydrophobic side-chains
within .alpha.-helixes of peptides and proteins)
IT 52-90-4, Cysteine, biological studies 56-41-7, Alanine, biological
studies 60-18-4, Tyrosine, biological studies 61-90-5, Leucine,
biological studies 63-68-3, Methionine, biological studies
63-91-2, Phenylalanine, biological studies 71-00-1, Histidine,
biological studies 72-18-4, Valine, biological studies 73-22-3,
Tryptophan, biological studies 73-32-5, Isoleucine, biological
studies
RL: BPR (Biological process); PRP (Properties); BIOL (Biological
study); PROC (Process)
(interactions between hydrophobic side-chains within
.alpha.-helixes of peptides and proteins)
L3 ANSWER 6 OF 46 CA COPYRIGHT 1996 ACS
AN 123:5053 CA
TI Evaluation of interactions between residues in .alpha.-helices by
exhaustive conformational search
AU Creamer, Trevor P.; Srinivasan, Rajgopal; ***Rose, George D.***
CS Sch. of Medicine, Washington Univ., St. Louis, MO, 63110, USA
SO Tech. Protein Chem. VI, [Pap. Symp. Protein Soc.], 8th (1995),
Meeting Date 1994, 443-50. Editor(s): Crabb, John W.. Publisher:
Academic, San Diego, Calif.
CODEN: 61MDAG
DT Conference
LA English
CC 9-16 (Biochemical Methods)
Section cross-reference(s): 6
AB Exhaustive serach techniques can be used to successfully model the
interactions and small motifs that are characteristic of protein
structure.
ST interaction residue alpha helix exhaustive conformation
IT Conformation and Conformers
Simulation and Modeling, physicochemical
(evaluation of interactions between residues in .alpha.-helixes
by exhaustive conformational search)
IT Proteins, properties
RL: PRP (Properties)
(evaluation of interactions between residues in .alpha.-helixes
by exhaustive conformational search)
IT Conformation and Conformers
(.alpha.-helical, evaluation of interactions between residues in
.alpha.-helixes by exhaustive conformational search)
L3 ANSWER 7 OF 46 CA COPYRIGHT 1996 ACS
AN 122:308962 CA
TI Sequence determinants of the capping box, a stabilizing motif at the
N-termini of .alpha.-helixes
AU Seale, Jeffrey W.; Srinivasan, Rajgopal; ***Rose, George D.***
CS Dep. Biochem. Mol. Biophys., Washington Univ. Sch. Med., St. Louis,
MO, 63110, USA
SO Protein Sci. (1994), 3(10), 1741-5
CODEN: PRCIEI; ISSN: 0961-8368
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB The capping box, a recurrent hydrogen bonded motif at the N-termini
of .alpha.-helixes, caps 2 of the initial 4 backbone amide hydrogen
donors of the helix (Harper ET, Rose GD, 1993, Biochem. 32:
7605-7609). In detail, the side chain of the first helical residue
forms a hydrogen bond with the backbone of the fourth helical
residue and, reciprocally, the side chain of the fourth residue
forms a hydrogen bond with the backbone of the first residue. The
authors now enlarge the earlier definition of this motif to include
an accompanying hydrophobic interaction between residues that
bracket the capping box sequence on either side. The expanded box
motif-in which 2 hydrogen bonds and a hydrophobic interaction are
localized within 6 consecutive residues - resembles a glycine-based
capping motif found at helix C-termini (Aurora R, Srinivasan R, Rose
GD, 1994, Science 264:1126-1130).
ST protein conformation helix capping box
IT Proteins, specific or class
RL: BSU (Biological study, unclassified); PEP (Physical, engineering
or chemical process); PRP (Properties); BIOL (Biological study);
PROC (Process)
(capping box-contg.; sequence determinants of capping box - a
stabilizing motif at N-termini of .alpha.-helixes)
IT Hydrogen bond
(sequence determinants of capping box - a stabilizing motif at
N-termini of .alpha.-helixes)
IT Conformation and Conformers
(.alpha.-helical, sequence determinants of capping box - a
stabilizing motif at N-termini of .alpha.-helixes)
L3 ANSWER 8 OF 46 CA COPYRIGHT 1996 ACS
AN 122:74854 CA
TI .alpha.-Helix-forming propensities in peptides and proteins
AU Creamer, Trevor P.; ***Rose, George D.***
CS Sch. Med., Washington Univ., St. Louis, MO, 63110, USA
SO Proteins: Struct., Funct., Genet. (1994), 19(2), 85-97
CODEN: PSFGEY; ISSN: 0887-3585
DT Journal
LA English
CC 6-3 (General Biochemistry)
Section cross-reference(s): 9
AB Much effort has been invested in seeking to understand the thermodn.
basis of helix stability in both peptides and proteins. Recently,
several groups have measured the helix-forming propensities of
individual residues. Using Monte Carlo computer simulations, the
authors tested the hypothesis that these differences in measured
helix-forming propensity are due primarily to loss of side chain
conformational entropy upon helix formation (Creamer, T. P., Rose,
G. D. Proc. Natl. Acad. Sci. U.S.A. 89:5937-5941, 1992). The
previous study employed a rigid helix backbone, which is here
generalized to a completely flexible helix model to ensure that
earlier results were not a methodol. artifact. Using this flexible
model, side chain rotamer distributions and entropy losses are
calcd. and shown to agree with those obtained earlier. The authors
note that the side chain conformational entropy calcd. for Trp in
the previous study was in error; a cor. value is presented.
Extending earlier work, calcd. entropy losses are found to correlate
strongly with recent helix propensity scales derived from
substitutions made within protein helixes. In contrast, little
correlation is found between these helix propensity scales and the
accessible surface area buried upon formation of a model polyalanyl
.alpha.-helix. Taken in sum, the results indicate that loss of side
chain entropy is a major determinant of the helix-forming tendency
of residues in both peptide and protein helixes.
ST conformation helix protein peptide entropy
IT Peptides, biological studies
RL: BSU (Biological study, unclassified); PRP (Properties); BIOL
(Biological study)
(.alpha.-helix-contg.; .alpha.-helix-forming propensities in
peptides and proteins)
IT Amino acids, biological studies
RL: BSU (Biological study, unclassified); PRP (Properties); BIOL
(Biological study)
(.alpha.-helix-forming propensities in peptides and proteins)
IT Simulation and Modeling, biological
(Monte Carlo, .alpha.-helix-forming propensities in peptides and
proteins)
IT Entropy
Potential energy and function
(conformational, .alpha.-helix-forming propensities in peptides
and proteins)
IT Conformation and Conformers
(.alpha.-helical, .alpha.-helix-forming propensities in peptides
and proteins)
IT Proteins, specific or class
RL: BSU (Biological study, unclassified); PRP (Properties); BIOL
(Biological study)
(.alpha.-helix-contg., .alpha.-helix-forming propensities in
peptides and proteins)
IT 56-41-7, Alanine, biological studies 60-18-4, Tyrosine, biological
studies 61-90-5, Leucine, biological studies 63-68-3,
Methionine, biological studies 63-91-2, Phenylalanine, biological
studies 72-18-4, Valine, biological studies 73-22-3, Tryptophan,
biological studies 73-32-5, Isoleucine, biological studies
25191-17-7, Poly(alanine) 25213-34-7, Poly(alanine)
RL: BSU (Biological study, unclassified); PRP (Properties); BIOL
(Biological study)
(.alpha.-helix-forming propensities in peptides and proteins)
L3 ANSWER 9 OF 46 CA COPYRIGHT 1996 ACS
AN 122:26214 CA
TI The T-to-R transformation in hemoglobin: a reevaluation
AU Srinivasan, Rajgopal; ***Rose, George D.***
CS Dep. Biochem. Mol. Biophys., Washington Univ. Sch. Med., St. Louis,
MO, 63110, USA
SO Proc. Natl. Acad. Sci. U. S. A. (1994), 91(23), 11113-17
CODEN: PNASA6; ISSN: 0027-8424
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB The relation between the T, R, and R2 quaternary forms of Hb is
examd. by computational expts. Contrary to previous suggestions,
the authors propose that the R quaternary form may lie on the
pathway from T to R2. This proposal is consistent with four
independent observations. (I) Difference distance maps are used to
identify those parts of the mol. that undergo conformational change
upon oxygenation. The simplest interpretation of these maps
brackets R between T and R2. (Ii) Linear interpolation from T to R2
passes through R. (Iii) The well-known "switch" region (so called
because, upon transition between the T and R quaternary forms, a
residue from the .beta.2 subunit toggles between two stable
positions within the .alpha.1 subunit) progresses from T through R
to R2, successively. (I.v.) A hitherto-undocumented feature,
diagnostic of the R structure, is noted within the .alpha. subunit:
upon transformation from T to R, the .beta.-turns at the amino
termini of the E and F helixes flip from one turn type to another.
Upon transformation from R to R2, the latter turn-a strained
conformation-flips back again.
ST Hb quaternary structure conformation transition
IT Conformation and Conformers
Quaternary structure
(reevaluation of T-to-R transformation in Hb)
IT Hemoglobins
RL: BPR (Biological process); BSU (Biological study, unclassified);
PRP (Properties); BIOL (Biological study); PROC (Process)
(reevaluation of T-to-R transformation in Hb)
L3 ANSWER 10 OF 46 CA COPYRIGHT 1996 ACS
AN 122:3949 CA
TI Molten globular characteristics of the native state of apomyoglobin
AU Lin, Laura; Pinker, Rachel J.; Forde, Kirk; ***Rose, George D.***
; Kallenbach, Neville R.
CS Dept. Chemistry, New York Univ., New York, NY, 10003, USA
SO Nat. Struct. Biol. (1994), 1(7), 447-52
CODEN: NSBIEW; ISSN: 1072-8368
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB Apomyoglobin (apoMb) is a natural intermediate in biosynthesis of
Mb, and has some structural features in common with the heme-contg.
native state. Unfolding or refolding studies of apoMb have
identified a molten globule intermediate at acid pH. Here, it is
shown that both the native state of apoMb and the molten globule
intermediate have highly plastic structures. Substitution of single
amino acids on the surface or in the interior of helixes in the
native protein produce dramatic changes in the helix content and Trp
emission of apoMb at neutral and acidic pH. The signals from the
intermediate and native apoMb correlate closely suggesting that
apoMb itself has a molten globule-like character, its structure
representing a population of interconverting substrates rather than
a fixed conformation.
ST apomyoglobin molten globule conformation
IT Conformation and Conformers
(molten globule; molten globular characteristics of the native
state of apomyoglobin)
IT Myoglobins
RL: PRP (Properties)
(apo-, molten globular characteristics of the native state of
apomyoglobin)
L3 ANSWER 11 OF 46 CA COPYRIGHT 1996 ACS
AN 121:295152 CA
TI Protein folding: predicting predicting
AU ***Rose, George D.*** ; Creamer, Trevor P.
CS Sch. Med., Washington Univ., St. Louis, MO, 63110, USA
SO Proteins: Struct., Funct., Genet. (1994), 19(1), 1-3
CODEN: PSFGEY; ISSN: 0887-3585
DT Journal; General Review
LA English
CC 6-0 (General Biochemistry)
AB A review, with 19 refs., discussing the perspectives of protein
folding and its prediction.
ST review protein folding prediction
IT Conformation and Conformers
(prediction of protein folding)
IT Proteins, properties
RL: PRP (Properties)
(prediction of protein folding)
L3 ANSWER 12 OF 46 CA COPYRIGHT 1996 ACS
AN 121:102318 CA
TI Rules for .alpha.-helix termination by glycine
AU Aurora, Rajeev; Srinivasan, Rajgopal; ***Rose, George D.***
CS Sch. Med., Washington Univ., St. Louis, MO, 63110, USA
SO Science (Washington, D. C.) (1994), 264(5162), 1126-30
CODEN: SCIEAS; ISSN: 0036-8075
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB A predictive rule for protein folding is presented that involves two
recurrent glycine-based motifs that cap the carboxyl termini of
.alpha. helixes. In proteins, helixes that terminated in glycine
residues were found predominantly in one of these two motifs. These
glycine structures had a characteristic pattern of polar and apolar
residues. Visual inspection of known helical sequences was
sufficient to distinguish the two motifs from each other and from
internal glycines that fail to terminate helixes. These glycine
motifs - in which the local sequence selects between available
structures - represent an example of a stereochem. rule for protein
folding.
ST protein helix conformation glycine carboxy terminus
IT Proteins, properties
RL: PRP (Properties)
(.alpha.-helical conformation of, glycine-based capping motifs in
carboxy termini of)
IT Conformation and Conformers
(.alpha.-helical, of proteins, glycine-based capping motifs in
carboxy termini of)
IT 56-40-6, Glycine, properties
RL: PRP (Properties)
(protein .alpha.-helical conformations contg. capping motifs
based on, in carboxy terminus)
L3 ANSWER 13 OF 46 CA COPYRIGHT 1996 ACS
AN 119:219951 CA
TI Effects of alanine substitutions in .alpha.-helixes of sperm whale
myoglobin on protein stability
AU Pinker, Rachel J.; Lin, Laura; ***Rose, George D.*** ;
Kallenbach, Neville R.
CS Dep. Chem., New York Univ., New York, NY, 10003, USA
SO Protein Sci. (1993), 2(7), 1099-105
CODEN: PRCIEI; ISSN: 0961-8368
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB The peptide backbones in folded native proteins contain distinctive
secondary structures, .alpha.-helixes, .beta.-sheets, and turns,
with significant frequency. One question that arises in folding is
how the stability of this structure relates to that of the protein
as a whole. To address this question, the authors substituted the
.alpha.-helix-stabilizing alanine side chain at 16 selected sites in
the sequence of sperm whale myoglobin, 12 at helical sites on the
surface of the protein, and 4 at obviously internal sites.
Substitution of alanine for bulky side chains at internal sites
destabilizes the protein, as expected if packing interactions are
disrupted. Alanine substitutions do not uniformly stabilize the
protein, either in capping positions near the ends of helixes or at
mid-helical sites near the surface of myoglobin. When cor. for the
extent of exposure of each side chain replaced by alanine at a
mid-helix position, alanine replacement still has no clear effect in
stabilizing the native structure. Thus linkage between the
stabilization of secondary structure and tertiary structure in
myoglobin cannot be demonstrated, probably because of the relatively
small free energy differences between side chains in stabilizing
isolated helix. By contrast, about 80% of the variance in free
energy obsd. can be accounted for by the loss in buried surface area
of the native residue substituted by alanine. The differential free
energy of helix stabilization does not account for any addnl.
variation.
ST myoglobin helix conformation stability alanine substitution; protein
helix folding stability alanine substitution
IT Myoglobins
RL: BIOL (Biological study)
(.alpha.-helical regions of, alanine substitutions in, protein
stability response to)
IT Proteins, properties
RL: PRP (Properties)
(.alpha.-helical regions of, alanine substitutions in, stability
response to)
IT Free energy
(conformational, of myoglobin .alpha.-helical regions, alanine
substitutions effect on, tertiary structure stability in relation
to)
IT Conformation and Conformers
(tertiary, of proteins, secondary structure role in stability of)
IT Conformation and Conformers
(.alpha.-helical, of proteins, alanine substitutions in, protein
stability response to)
IT 56-41-7, Alanine, properties
RL: PRP (Properties)
(in protein .alpha.-helical regions, tertiary structure stability
dependence on)
L3 ANSWER 14 OF 46 CA COPYRIGHT 1996 ACS
AN 119:133548 CA
TI Hydrogen bonding, hydrophobicity, packing, and protein folding
AU ***Rose, George D.***
CS Sch. Med., Washington Univ., St. Louis, MO, 63110, USA
SO Annu. Rev. Biophys. Biomol. Struct. (1993), 22, 381-415
CODEN: ABBSE4; ISSN: 1056-8700
DT Journal; General Review
LA English
CC 6-0 (General Biochemistry)
AB A review, with 189 refs., of protein folding and stability and the
roles of hydrogen bonding, hydrophobicity and internal packing in
protein folding.
ST review protein conformation folding; hydrogen bond protein
conformation folding review; hydrophobicity protein conformation
folding review; packing protein conformation folding review
IT Proteins, properties
RL: PRP (Properties)
(conformation of, folding of)
IT Hydrogen bond
Hydrophobicity
(in protein conformational folding, role of)
IT Conformation and Conformers
(of proteins, folding of)
IT 1333-74-0
RL: BIOL (Biological study)
(hydrogen bond, in protein conformational folding, role of)
IT 7732-18-5
RL: BIOL (Biological study)
(hydrophobicity, in protein conformational folding, role of)
L3 ANSWER 15 OF 46 CA COPYRIGHT 1996 ACS
AN 119:66031 CA
TI Helix stop signals in proteins and peptides: The capping box
AU Harper, Edwin T.; ***Rose, George D.***
CS Sch. Med., Washington Univ., St. Louis, MO, 63110, USA
SO Biochemistry (1993), 32(30), 7605-9
CODEN: BICHAW; ISSN: 0006-2960
DT Journal
LA English
CC 6-3 (General Biochemistry)
OS CJACS-IMAGE; CJACS
AB The .alpha.-helix (Pauling, L.; et al., 1951) is a common motif in
both proteins and peptides. Despite intense investigation,
predictive understanding of helixes is still lacking. A recent
hypothesis [Presta, L. G.; Rose, G. D., 1988) proposed that the
structural specificity of helixes resides, in part, in those
residues that flank helix termini. If so, then signals that arrest
helix propagation, i.e., helix stop signals, should be found among
these flanking residues. Evidence is presented for the existence of
one such signal, a reciprocal backbone-side-chain hydrogen-bonding
interaction, dubbed the capping box. In proteins, the capping box
is found uniquely at helix N-termini. In peptides, the capping box
can function as a helix stop signal.
ST helix alpha stop signal peptide protein
IT Amino acids, biological studies
RL: BIOL (Biological study)
(of .alpha.-helix stop signal, of peptides and proteins)
IT Peptides, properties
RL: PRP (Properties)
(.alpha.-helix of, stop signal for, reciprocal
backbone-side-chain hydrogen-bonding interaction of capping box
as)
IT Proteins, properties
RL: PRP (Properties)
(.alpha.-helix of, stop signal for, reciprocal
backbone-side-chain hydrogen-bonding interaction of capping box
at helix N-terminus as)
IT Conformation and Conformers
(.alpha.-helical, of peptides and proteins, stop signal for,
reciprocal backbone-side-chain hydrogen-bonding interaction of
capping box as)
IT 56-45-1, Serine, biological studies 56-84-8, Aspartic acid,
biological studies 56-85-9, Glutamine, biological studies
56-86-0, Glutamic acid, biological studies 70-47-3, Asparagine,
biological studies 71-00-1, Histidine, biological studies
72-19-5, Threonine, biological studies
RL: BIOL (Biological study)
(of .alpha.-helix stop signal, of peptides and proteins)
L3 ANSWER 16 OF 46 CA COPYRIGHT 1996 ACS
AN 118:96564 CA
TI Protein folding. What's the question?
AU Lattman, Eaton E.; ***Rose, George D.***
CS Sch. Med., Johns Hopkins Univ., Baltimore, MD, 21205, USA
SO Proc. Natl. Acad. Sci. U. S. A. (1993), 90(2), 439-41
CODEN: PNASA6; ISSN: 0027-8424
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB The folding reactions of many small, globular proteins exhibit
two-state kinetics, in which the folded and unfolded states
interconvert readily without observable intermediates. Typically,
the free energy difference, .DELTA.G, between the native and
denatured states of such a protein is quite small, lying in the
range of approx. -5 to -15 kcal/mol. Under these circumstances, a
population of native-like mols. will persist, even in the presence
of mutations sufficiently destabilizing to change the sign of
.DELTA.G. Therefore, it is not energy per se that dets.
conformation. A corollary to this argument is that specificity -
not stability - would be the more informative focus in future
folding studies.
ST protein conformation folding determinant
IT Proteins, properties
RL: PRP (Properties)
(conformation of, determinants of folding in)
IT Conformation and Conformers
(of proteins, determinants of folding in)
IT Free energy
(conformational, of proteins, folding determinants in relation
to)
L3 ANSWER 17 OF 46 CA COPYRIGHT 1996 ACS
AN 118:34647 CA
TI Hydrogen bonding in globular proteins
AU Stickle, Douglas F.; Presta, Leonard G.; Dill, Ken A.; ***Rose,
George D.***
CS Coll. Med., Pennsylvania State Univ., Hershey, PA, 17033, USA
SO J. Mol. Biol. (1992), 226(4), 1143-59
CODEN: JMOBAK; ISSN: 0022-2836
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB A global census of the hydrogen bonds in 42 x-ray-elucidated
proteins was taken and the following demog. trends were identified.
Most hydrogen bonds are local, i.e. between partners that are close
in sequence, the primary exception being hydrogen-bonded ions pairs.
Most hydrogen bonds are between backbone atoms in the protein, an
av. of 68%. All proteins studied have extensive hydrogen-bonded
secondary structure, an av. of 82%. Almost all backbone hydrogen
bonds are within single elements of secondary structure. An approx.
rule of thirds applies: slightly more than one-third (37%) form
i.fwdarw.i-3 hydrogen bonds, almost one-third (32%) form
i.fwdarw.i-4 hydrogen bonds, and slightly less than one-third (26%)
reside in paired strands of .beta.-sheet. The remaining 5% are not
wholly within an individual helix, turn or sheet. Side-chain to
backbone hydrogen bonds are clustered at helix-capping positions.
An extensive network of hydrogen bonds is present in helixes. To a
close approxn., the total no. of hydrogen bonds is a simple function
of a protein's helix and sheet content. A unique quantity, termed
the reduced no. of hydrogen bonds, is defined as the max. no. of
hydrogen bonds possible when every donor:acceptor pair is
constrained to be 1:1. This quantity scales linearly with chain
length, with 0.71 reduced hydrogen bond per residue. Implications
of these results for pathways of protein folding are discussed.
ST protein globular hydrogen bond folding; conformation folding
globular protein hydrogen bond
IT Hydrogen bond
(of globular proteins, quantity and classification and patterns
of)
IT Conformation and Conformers
(of proteins, hydrogen bonding in, protein folding in relation
to)
IT Proteins, specific or class
RL: PEP (Physical, engineering or chemical process); PRP
(Properties); PROC (Process)
(globular, hydrogen bonding in, protein folding in relation to)
IT Conformation and Conformers
(secondary, of proteins, hydrogen bonding in, quantity and
classification and patterns of)
IT 1333-74-0
RL: BIOL (Biological study)
(hydrogen bond, of globular proteins, quantity and classification
and patterns of)
L3 ANSWER 18 OF 46 CA COPYRIGHT 1996 ACS
AN 117:126745 CA
TI Side-chain entropy opposes .alpha.-helix formation but rationalizes
experimentally determined helix-forming propensities
AU Creamer, Trevor P.; ***Rose, George D.***
CS Dep. Biochem. Biophys., Univ. North Carolina, Chapel Hill, NC,
27599-7260, USA
SO Proc. Natl. Acad. Sci. U. S. A. (1992), 89(13), 5937-41
CODEN: PNASA6; ISSN: 0027-8424
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB In recent host-guest studies, the helix-forming tendencies of amino
acid residues have been quantified. Here, the hypothesis that these
measured helix-forming propensities are due primarily to
conformational restrictions imposed upon residue side chains by the
helix itself are explored. This proposition is tested by calcg. the
extent to which the bulky helix backbone freezes out available
degrees of freedom in helix side chains. Specifically, for a series
of apolar residues, the difference in configurational entropy,
.DELTA.S, between each side chain in the unfolded state and in the
.alpha.-helical state is obtained from a simple Monte Carlo calcn.
These computed entropy differences are then compared with the exptl.
detd. values. Measured and calcd. values are found to be in close
agreement for naturally occurring amino acids and in total
disagreement for non-natural amino acids. In the calcn.,
.DELTA.SAla = 0. The rank order of entropy loss for the series of
natural apolar side chains under consideration is Ala < Leu < Trp <
Met < Phe < Ile < Tyr < Val. Among these, none favor helix
formation; Ala is neutral, and all remaining residues are
unfavorable to varying degrees. Thus, applied to side chains, the
term helix preference is a misnomer. While side chain-side chain
interactions may modulate stability in some instances, these results
indicate that the drive to form helices must originate in the
backbone, consistent with Pauling's view of four decades ago
(Pauling, L., et al., 1951).
ST protein helix conformation side chain entropy
IT Amino acids, properties
RL: PRP (Properties)
(entropy of side-chains of, of proteins, in folded and helical
state, helix-forming propensity in relation to)
IT Proteins, properties
RL: PRP (Properties)
(helix formation by, loss of side-chain entropy role in)
IT Simulation and Modeling, physicochemical
(of amino acid side-chain entropy, protein helix formation effect
on)
IT Entropy
(configurational, of amino acid side-chains in unfolded and
helical state, helix-forming propensity in relation to)
IT Conformation and Conformers
(.alpha.-helical, formation of, in proteins, loss of side-chain
entropy role in)
IT 56-41-7, Alanine, properties 60-18-4, Tyrosine, properties
61-90-5, Leucine, properties 63-68-3, Methionine, properties
63-91-2, Phenylalanine, properties 72-18-4, Valine, properties
73-22-3, Tryptophan, properties 73-32-5, Isoleucine, properties
80-60-4, .alpha.-Aminobutyric acid 327-57-1, Norleucine
6600-40-4, Norvaline
RL: PRP (Properties)
(entropy of side-chains of, of protein, in unfolded and helical
state)
L3 ANSWER 19 OF 46 CA COPYRIGHT 1996 ACS
AN 115:44515 CA
TI The protein-folding problem: the native fold determines packing,
but does packing determine the native fold?
AU Behe, Michael J.; Lattman, Eaton E.; ***Rose, George D.***
CS Coll. Med., Pennsylvania State Univ., Hershey, PA, 17033, USA
SO Proc. Natl. Acad. Sci. U. S. A. (1991), 88(10), 4195-9
CODEN: PNASA6; ISSN: 0027-8424
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB A globular protein adopts its native three-dimensional structure
spontaneously under physiol. conditions. This structure is
specified by a stereochem. code embedded within the amino acid
sequence of that protein. Elucidation of this code is a major,
unsolved challenge, known as the protein-folding problem. A crit.
aspect of the code is thought to involve mol. packing. Globular
proteins have high packing densities, a consequence of the fact that
residue side chains within the mol. interior fit together with an
exquisite complementarity, like pieces of a three-dimensional jigsaw
puzzle. Such packing interactions are widely viewed as the
principal determinant of the native structure. To test this view,
the authors analyzed proteins of known structure for the presence of
preferred interactions, reasoning that if side-chain complementarity
is an important source of structural specificity, then sets of
residues that interact favorably should be apparent. The anal.
leads to the surprising conclusion that high packing densities, so
characteristic of globular proteins, are readily attainable among
clusters of the naturally occurring hydrophobic amino acid residues.
It is anticipated that this realization will simplify approaches to
the protein-folding problem.
ST globular protein folding side chain packing; conformation globular
protein folding packing
IT Conformation and Conformers
(of globular proteins, folding of, hydrophobic side-chain packing
in relation to)
IT Amino acids, biological studies
RL: BIOL (Biological study)
(of globular proteins, hydrophobic side-chains of, packing of,
protein folding in relation to)
IT Proteins, specific or class
RL: BIOL (Biological study)
(globular, folding of, hydrophobic side chain packing in relation
to)
L3 ANSWER 20 OF 46 CA COPYRIGHT 1996 ACS
AN 114:19620 CA
TI Hydrophobicity of amino acid subgroups in proteins
AU Lesser, Glenn J.; ***Rose, George D.***
CS Coll. Med., Pennsylvania State Univ., Hershey, PA, 17033, USA
SO Proteins: Struct., Funct., Genet. (1990), 8(1), 6-13
CODEN: PSFGEY; ISSN: 0887-3585
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB Protein folding studies often utilize areas and vols. to assess the
hydrophobic contribution to conformational free energy (Richards,
F.M., 1977). The mean area buried upon folding was calcd. for every
chem. group in each residue within a set of x-ray elucidated
proteins. These measurements, together with a std. state cavity
size for each group, are documented. It is obsd. that, on av., each
type of group buries a const. fraction of its std. state area. The
mean area buried by most, though not all, groups can be closely
approximated by summing contributions from the 3 characteristic
parameters corresponding to 3 atom types: (1) C or S, which turn out
to be 86% buried, on av.; (2) neutral O or N, which are 40% buried,
on av.; and (3) charged O or N, which are 32% buried, on av.
ST protein amino acid subgroup hydrophobicity folding
IT Surface area
(amino acids and subgroups in proteins, hydrophobicity and
folding in relation to)
IT Amino acids, properties
RL: PRP (Properties)
(hydrophobicity of subgroups and, in protein folding,
solvent-accessible surface area in relation to)
IT Hydrophobicity
(of amino acids and subgroups in globular proteins, folding
dependence on)
IT Conformation and Conformers
(of globular proteins, folding of, amino acid subgroup
hydrophobicity in relation to)
IT Proteins, specific or class
RL: BIOL (Biological study)
(globular, hydrophobicity of amino acid subgroup in, folding in
relation to)
IT Functional groups
(hydrophilic, solvent-accessible area of, in globular proteins,
folding in relation to)
IT Functional groups
(hydrophobic, solvent-accessible area of, in globular proteins,
folding in relation to)
IT 7732-18-5
RL: BIOL (Biological study)
(hydrophobicity, of amino acids and subgroups in globular
proteins, folding dependence on)
IT 52-90-4, L-Cysteine, properties 56-40-6, Glycine, properties
56-41-7, L-Alanine, properties 56-45-1, L-Serine, properties
56-84-8, L-Aspartic acid, properties 56-85-9, L-Glutamine,
properties 56-86-0, L-Glutamic acid, properties 56-87-1,
L-Lysine, properties 56-89-3, L-Cystine, properties 60-18-4,
L-Tyrosine, properties 61-90-5, L-Leucine, properties 63-68-3,
L-Methionine, properties 63-91-2, L-Phenylalanine, properties
70-47-3, L-Asparagine, properties 71-00-1, L-Histidine, properties
72-18-4, L-Valine, properties 72-19-5, L-Threonine, properties
73-22-3, L-Tryptophan, properties 73-32-5, L-Isoleucine,
properties 74-79-3, L-Arginine, properties 147-85-3, L-Proline,
properties
RL: PRP (Properties)
(surface area of, in protein folding, hydrophobicity in relation
to)
L3 ANSWER 21 OF 46 CA COPYRIGHT 1996 ACS
AN 109:224780 CA
TI Protein folding: new twists
AU Fetrow, Jacquelyn S.; Zehfus, Micheal H.; ***Rose, George D.***
CS Sch. Med., Univ. Rochester, Rochester, NY, 14642, USA
SO Bio/Technology (1988), 6(2), 167-71
CODEN: BTCHDA; ISSN: 0733-222X
DT Journal; General Review
LA English
CC 6-0 (General Biochemistry)
AB A review, with 46 refs., on protein folding and the proposed
existence of an explicit stereochem. code for protein assembly.
ST review protein conformation folding
IT Proteins, properties
RL: PRP (Properties)
(conformation and folding of, genetic code in relation to)
IT Protein formation
(folding patterns during, genetic code in relation to)
IT Conformation and Conformers
(of proteins, genetic code in relation to)
IT Genetic code
(protein folding patterns in relation to)
L3 ANSWER 22 OF 46 CA COPYRIGHT 1996 ACS
AN 109:69048 CA
TI Helix signals in proteins
AU Presta, Leonard G.; ***Rose, George D.***
CS Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA, 17033,
USA
SO Science (Washington, D. C., 1883-) (1988), 240(4859), 1632-41
CODEN: SCIEAS; ISSN: 0036-8075
DT Journal
LA English
CC 6-3 (General Biochemistry)
Section cross-reference(s): 7
AB The helix hypothesis introduced here states that a necessary
condition for helix formation is the presence of residues flanking
the helix termini whose side chains can form H bonds with the
initial 4-helix > N-H groups and final 4-helix > C-O groups; these 8
groups would otherwise lack intrahelical partners. This simple
hypothesis implies the existence of a stereochem. code in which
certain sequences have the H-bonding capacity to function as helix
boundaries and thereby enable the helix to form autonomously. The
3-dimensional structure of a protein is a consequence of the genetic
code, but the rules relating sequence to structure are still
unknown. The ensuing anal. supports the idea that a stereochem.
code for the .alpha. helix resides in its boundary residues.
ST protein conformation helix sequence
IT Amino acids, properties
RL: PRP (Properties)
(hydrogen bonding of, in .alpha.-helix conformation of proteins,
prediction of)
IT Hydrogen bond
(in .alpha.-helix conformation of proteins, peptide sequence
prediction of)
IT Enzymes
Proteins, properties
RL: BIOL (Biological study)
(.alpha.-helix conformation in, sequence prediction of, flanking
residues role in)
IT Protein sequences
(.alpha.-helix conformation of proteins prediction by, flanking
residues role in)
IT Conformation and Conformers
(.alpha.-helical, in proteins, sequence prediction of, flanking
residues role in)
IT 1333-74-0
RL: BIOL (Biological study)
(hydrogen bond, in .alpha.-helix conformation of proteins,
peptide sequence prediction of)
L3 ANSWER 23 OF 46 CA COPYRIGHT 1996 ACS
AN 108:2770 CA
TI Hydrophobicity profiles revisited
AU Dworkin, Jonathan E.; ***Rose, George D.***
CS Milton S. Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA,
17033, USA
SO Methods Protein Sequence Anal., [Proc. Int. Conf.], 6th (1987),
Meeting Date 1986, 573-86. Editor(s): Walsh, Kenneth A. Publisher:
Humana, Clifton, N. J.
CODEN: 56DFAZ
DT Conference; General Review
LA English
CC 9-0 (Biochemical Methods)
Section cross-reference(s): 6
AB A review with 25 refs. The assumptions and parameters of
hydrophobicity profiles are discussed. Methodol. is described that
allows error bars and confidence limits to be derived. A detailed
comparison with exptl. data from x-ray elucidated proteins is also
presented.
ST review protein hydrophobicity profile
IT Proteins, properties
RL: PRP (Properties)
(hydrophobicity profiles of, construction of)
IT Hydrophobicity
(of proteins, profiles of, construction of)
IT 7732-18-5
RL: ANST (Analytical study)
(hydrophobicity, of proteins, profiles of, construction of)
L3 ANSWER 24 OF 46 CA COPYRIGHT 1996 ACS
AN 106:194168 CA
TI Immune recognition of proteins: conclusions, dilemmas and enigmas
AU Smith, John A.; ***Rose, George D.***
CS Dep. Mol. Biol., Massachusetts Gen. Hosp., Boston, MA, 02115, USA
SO BioEssays (1987), 6(3), 112-16
CODEN: BIOEEJ
DT Journal; General Review
LA English
CC 15-0 (Immunochemistry)
AB A review with 29 refs. of the structure of antigenic sites and their
mol. interactions with antibodies, major histocompatibility
complex-restriction elements, and T-lymphocyte receptors.
ST review antigen structure antibody lymphocyte
IT Antibodies
RL: BIOL (Biological study)
(antigen recognition by, structure in)
IT Receptors
RL: BIOL (Biological study)
(for antigen, of T-cell, structure in relation to)
IT Conformation and Conformers
(of antigens, antibody and T-lymphocyte recognition in relation
to)
IT Antigens
RL: PRP (Properties)
(structure of, antibody and T-cell receptor recognition in
relation to)
IT Lymphocyte
(T-, antigen recognition by, structure in)
IT Antigens
RL: BIOL (Biological study)
(major histocompatibility complex, antigen recognition by, T-cell
receptor structure in relation to)
L3 ANSWER 25 OF 46 CA COPYRIGHT 1996 ACS
AN 106:45920 CA
TI Loops in globular proteins: a novel category of secondary structure
AU Leszczynski, Jacquelyn F.; ***Rose, George D.***
CS Milton S. Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA,
17033, USA
SO Science (Washington, D. C., 1883-) (1986), 234(4778), 849-55
CODEN: SCIEAS; ISSN: 0036-8075
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB The protein loop, a novel category of nonregular secondary
structure, is a segment of contiguous polypeptide chain that traces
a loop-shaped path in 3-dimensional space; the main chain of an
idealized loop resembles the Greek letter .OMEGA.. A systematic
study was made of 67 proteins of known structure revealing 270
.OMEGA. loops. Although such loops are typically regarded as random
coil, they are, in fact, highly compact substructures and may also
be independent folding units. Loops are almost invariably situated
at the protein surface where they are poised to assume important
roles in mol. function and biol. recognition. They are often obsd.
to be modules of evolutionary exchange and are also natural
candidates for bioengineering studies.
ST loop conformation globular protein
IT Proteins, specific or class
RL: PRP (Properties)
(globular, loop conformation in)
IT Conformation and Conformers
(.OMEGA. loop, in globular proteins)
L3 ANSWER 26 OF 46 CA COPYRIGHT 1996 ACS
AN 105:149238 CA
TI Compact units in proteins
AU Zehfus, Michael H.; ***Rose, George D.***
CS Milton S. Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA,
17033, USA
SO Biochemistry (1986), 25(19), 5759-65
CODEN: BICHAW; ISSN: 0006-2960
DT Journal
LA English
CC 9-10 (Biochemical Methods)
Section cross-reference(s): 6, 7
OS CJACS
AB An explicit measure of geometric compactness called the coeff. of
compactness is introduced. This single value figure of merit
identifies those continuous segments of the polypeptide chain having
the smallest solvent-accessible surface area for their vol. These
segments are the most compact units of the protein, and the larger
ones correspond to conventional protein domains. To demonstrate the
plausibility of this approach as a method of identifying protein
domains, the measure is applied to lysozyme and RNase to discover
their constituent compact units. These units are then compared with
domains, subdomains, and modules found by other methods. To show
the sensitivity of the method, the measure is used to successfully
differentiate between native and deliberately misfolded proteins
[Novotny, J. et al., 1984]. Methods that utilize only backbone
atoms to define domains cannot distinguish between authentic and
misfolded mols. because their backbone conformations are virtually
superimposable. Compact units identified by this method exhibit a
hierarchic organization. Such an organization suggests possible
folding pathways that can be tested exptl.
ST compactness identification protein conformation; enzyme compact unit
detection; surface area protein coeff compactness
IT Immunoglobulins
RL: PRP (Properties)
(VL domain of, compactness of, identification of)
IT Nomenclature, new concepts
(coeff. of compactness)
IT Hemerythrins
Proteins
RL: ANST (Analytical study)
(compact units of, identification of, coeff. of compactness in)
IT Conformation and Conformers
(of proteins, compact units identification in, coeff. of
compactness for)
IT Surface area
(of proteins, normalized measure of, coeff. of compactness as)
IT 9001-63-2 9001-99-4
RL: ANST (Analytical study)
(compact units of, identification of, coeff. of compactness in)
L3 ANSWER 27 OF 46 CA COPYRIGHT 1996 ACS
AN 105:21279 CA
TI Molecular cartography of globular proteins with application to
antigenic sites
AU Fanning, David W.; Smith, John A.; ***Rose, George D.***
CS Milton S. Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA,
17033, USA
SO Biopolymers (1986), 25(5), 863-83
CODEN: BIPMAA; ISSN: 0006-3525
DT Journal
LA English
CC 9-10 (Biochemical Methods)
Section cross-reference(s): 6, 15
AB A method, mol. cartog., is introduced as a way to quantitate the
topog. structure of a protein surface. The method is applied to the
problem of antigenic determinants, and it is used to examine local
and global topog. of reported antigenic regions on the surface of
myoglobin and lysozyme. In nine antigenic sites taken from the
literature and studied in detail, no local property was found in
sites that was not also found in remaining regions of the surface.
However, a strong correlation was found between antigenic sites and
regions of the surface that are globally exposed. This finding
suggests that global exposure of the protein surface may play a
primary role in detg. the antigenic structure of the protein. Mol.
cartog. may be useful in other instances of protein-protein
interactions such as those between proteolytic enzymes and their
substrates.
ST globular protein topog cartog; antigenic site cartog globular
protein
IT Myoglobins
RL: ANST (Analytical study)
(cartog. of, antigenic sites in relation to)
IT Antigens
RL: ANST (Analytical study)
(determinants, cartog. in study of)
IT Surface structure
(of globular proteins, cartog. in study of)
IT Proteins
RL: ANST (Analytical study)
(globular, cartog. of, antigenic sites in relation to)
IT 9001-63-2
RL: ANST (Analytical study)
(cartog. of, antigenic sites in relation to)
L3 ANSWER 28 OF 46 CA COPYRIGHT 1996 ACS
AN 104:205063 CA
TI Algorithmic identification of antigenic determinants in proteins of
known structure
AU Fanning, David W.; ***Rose, George D.*** ; Smith, John A.
CS Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA, 17033,
USA
SO Pept.: Struct. Funct., Proc. Am. Pept. Symp., 9th (1985), 13-22.
Editor(s): Deber, Charles M.; Hruby, Victor J.; Kopple, Kenneth D.
Publisher: Pierce Chem. Co., Rockford, Ill.
CODEN: 54ZNAJ
DT Conference
LA English
CC 15-2 (Immunochemistry)
AB Protein topog. maps of myoglobin and lysozyme were constructed and
previously detd. antigenic sites were superimposed on the maps. The
known epitopes corresponded generally, but not perfectly, to highly
exposed regions of the mol. surface.
ST antigen site lysozyme myoglobin structure; mol structure antigen
lysozyme myoglobin
IT Myoglobins
RL: BIOL (Biological study)
(antigenic determinants in, identification of, from protein
topog. maps)
IT Antigens
RL: PROC (Process)
(identification of, from protein topog. maps of lysozyme and
myoglobin)
IT Conformation and Conformers
(of antigenic sites, of lysozyme and myoglobin, protein topog.
maps in relation to)
IT Molecular structure-biological activity relationship
(antigenic, of lysozyme and myoglobin, protein topog. maps in
relation to)
IT 9001-63-2
RL: BIOL (Biological study)
(antigenic determinants in, identification of, from protein
topog. maps)
L3 ANSWER 29 OF 46 CA COPYRIGHT 1996 ACS
AN 104:182766 CA
TI Fast approximations for accessible surface area and molecular volume
of protein segments
AU Zehfus, Micheal H.; Seltzer, Jack P.; ***Rose, George D.***
CS Milton S. Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA,
17033, USA
SO Biopolymers (1985), 24(12), 2511-19
CODEN: BIPMAA; ISSN: 0006-3525
DT Journal
LA English
CC 9-10 (Biochemical Methods)
Section cross-reference(s): 7
AB Equations are presented that approx. the accessible surface area of
a continuous protein segment using the surface area of an inertial
ellipsoid and that approx. the mol. vol. from the no. of nonhydrogen
atoms in the segment. These approxns., which are appropriate for
segments of 4 or more residues in length, are much faster to calc.
than the exact solns., yet suffer only a 3-8% error. Included in an
appendix are FORTRAN subroutines that calc. the surface area of an
ellipsoid from its 3 principal moments of inertia.
ST protein accessible surface area calcn; mol vol protein segment
computer
IT Proteins
RL: ANST (Analytical study)
(accessible surface are and mol. vol. detn. in segments of,
equations and computer programs for)
IT Ferredoxins
Flavodoxins
Myoglobins
Rubredoxins
RL: ANST (Analytical study)
(accessible surface area and mol. vol. detn. in segments of,
equations and computer programs for)
IT Computer program
(for accessible surface area and mol. vol. detn. in protein
segments)
IT Mathematics
(equations, for accessible surface area and mol. vol. detn. in
protein segments)
IT Proteins
RL: ANST (Analytical study)
(iron-contg., high-potential, accessible surface area and mol.
vol. detn. in segments of, equations and computer programs for)
IT 1393-38-0 9001-63-2 9001-73-4 9001-99-4 9002-07-7
9004-06-2 9007-43-6, properties 9026-81-7 9054-89-1
9087-70-1 11028-71-0 11075-17-5 39279-27-1
RL: ANST (Analytical study)
(accessible surface area and mol. vol. detn. in segments of,
equations and computer programs for)
L3 ANSWER 30 OF 46 CA COPYRIGHT 1996 ACS
AN 104:107541 CA
TI Antigenic determinants in proteins coincide with surface regions
accessible to large probes (antibody domains)
AU Novotny, Jiri; Handschumacher, Mark; Haber, Edgar; Bruccoleri,
Robert E.; Carlson, William B.; Fanning, David W.; Smith, John A.;
***Rose, George D.***
CS Harvard Med. Sch., Massachusetts General Hosp., Boston, MA, 02114,
USA
SO Proc. Natl. Acad. Sci. U. S. A. (1986), 83(2), 226-30
CODEN: PNASA6; ISSN: 0027-8424
DT Journal
LA English
CC 15-2 (Immunochemistry)
AB Surface areas on proteins that would be accessible to contacts with
large (1-nm radius) spherical probes were studied. Such spheres are
comparable in size to antibody domains that contain
antigen-combining sites. All the reported antigenic sites
correspond to segments particularly accessible to a large sphere.
The antigenic sites were also evident as the most prominently
exposed regions (hills and ridges) in contour maps of the
solvent-accessible (small-probe) surface. In myoglobin and
cytochrome c, virtually all of the van der Waals surface is
accessible to the large probe and therefore potentially antigenic;
in myohemerythrin, distinct large-probe-inacccessible, and
nonantigenic, surface regions are apparent. The correlation between
large-sphere-accessibility and antigenicity in myoglobin, lysozyme,
and cytochrome c appears to be better than that reported to exist
between antigenicity and segmental flexibility; i.e., surface
regions that are rigid often constitute antigenic epitopes, whereas
some of the flexible parts of the mols. do not appear antigenic. It
is proposed that the primary reason why certain polypeptide-chain
segments are antigenic is their exceptional surface exposure, making
them readily available for contacts with antigen-combining sites.
Exposure of these segments frequently results in high mobility and,
in consequence, to the reported correlation between antigenicity and
segmental flexibility.
ST protein antigenic determinant surface region
IT Myoglobins
RL: PRP (Properties)
(antigenic determinants on surface of, flexibility in relation
to)
IT Antigens
RL: BIOL (Biological study)
(determinants, on surface of proteins, flexibility in relation
to)
IT Molecular dynamics
Molecular structure, natural product
(of proteins, antigenic determinants of surface regions in
relation to)
IT Hemerythrins
RL: PRP (Properties)
(myo-, antigenic determinants on surface of, flexibility in
relation to)
IT 9001-63-2 9007-43-6, biological studies
RL: PRP (Properties)
(antigenic determinants on surface of, flexibility in relation
to)
L3 ANSWER 31 OF 46 CA COPYRIGHT 1996 ACS
AN 104:104495 CA
TI Molecular recognition in macromolecules
AU ***Rose, George D.*** ; Lee, Richard H.
CS Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA, 17033,
USA
SO Biophys. J. (1986), 49(1), 83-5
CODEN: BIOJAU; ISSN: 0006-3495
DT Journal; General Review
LA English
CC 6-0 (General Biochemistry)
AB A review, with 12 refs., of topol. features of biopolymer
recognition (assembly) sites and their modeling (by an algorithm).
ST review macromol mol recognition; assembly macromol recognition site
review; algorithm macromol recognition site review
IT Algorithm
(for biopolymer recognition site modeling)
IT Molecular association
(of biopolymers, recognition sites in, modeling of)
IT Biopolymers
RL: PRP (Properties)
(recognition sites of, modeling of)
L3 ANSWER 32 OF 46 CA COPYRIGHT 1996 ACS
AN 104:48304 CA
TI Automatic recognition of domains in globular proteins
AU ***Rose, George D.***
CS Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA, 17033,
USA
SO Methods Enzymol. (1985), 115(Diffr. Methods Biol. Macromol. Pt. B),
430-40
CODEN: MENZAU; ISSN: 0076-6879
DT Journal
LA English
CC 9-10 (Biochemical Methods)
Section cross-reference(s): 6, 7
AB The concept of structural domains in proteins and methods for
recognizing them are discussed. An algorithm devised to optimize
sequential subdivisions of a folded polypeptide chain into spatially
distinct regions without regard for chem. particulars, such as
residue type, H-bonding, or disulfide loops, is described.
ST protein domain recognition algorithm
IT Algorithm
(for protein structural domain automatic recognition)
IT Conformation and Conformers
(of proteins, automatic recognition of domains in)
IT Enzymes
RL: PRP (Properties)
(structural domains in, automatic recognition of)
IT Proteins
RL: PRP (Properties)
(globular, structural domains in, automatic recognition of)
L3 ANSWER 33 OF 46 CA COPYRIGHT 1996 ACS
AN 103:209012 CA
TI Turns in peptides and proteins
AU ***Rose, George D.*** ; Gierasch, Lila M.; Smith, John A.
CS Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA, USA
SO Adv. Protein Chem. (1985), 37, 1-109
CODEN: APCHA2; ISSN: 0065-3233
DT Journal; General Review
LA English
CC 6-0 (General Biochemistry)
AB A review with 383 refs., of the structural and functional roles of
conformational turns in proteins and peptides.
ST review protein peptide conformation turn
IT Proteins
Peptides, properties
RL: PRP (Properties)
(conformational turns in, functional and structural roles of)
IT Conformation and Conformers
(of peptides and proteins, turns in, structure and function in
relation to)
L3 ANSWER 34 OF 46 CA COPYRIGHT 1996 ACS
AN 103:174216 CA
TI Hydrophobicity of amino acid residues in globular proteins
AU ***Rose, George D.*** ; Geselowitz, Ari R.; Lesser, Glenn J.;
Lee, Richard H.; Zehfus, Micheal H.
CS Milton S. Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA,
17033, USA
SO Science (Washington, D. C., 1883-) (1985), 229(4716), 834-8
CODEN: SCIEAS; ISSN: 0036-8075
DT Journal
LA English
CC 6-3 (General Biochemistry)
Section cross-reference(s): 9
AB Two scales were derived, based on accessibility to solvent for
residues in proteins of known structure, to measure the av. area
that each residue buries upon folding. There is a simple linear
relation between the area a residue buries on folding and its
hydrophobicity, as measured by the .DELTA.G of transfer from water
to org. solvent. In addn., the residues can be divided into 3
groups on the basis of the deriv. of their mean fractional area
loss.
ST amino acid hydrophobicity globular protein; area amino acid protein
folding
IT Amino acids, properties
RL: PRP (Properties)
(hydrophobicity of, in globular proteins, surface area burying in
protein folding in relation to)
IT Surface area
(of amino acids, in globular protein folding, hydrophobicity in
relation to)
IT Hydrophobicity
(of amino acids, of globular proteins, surface area burying in
protein folding in relation to)
IT Free energy
(of folding, of globular proteins, amino acid surface area in
relation to)
IT Conformation and Conformers
(of globular proteins, hydrophobicity-surface area relations in)
IT Proteins
RL: BIOL (Biological study)
(globular, amino acid hydrophobicity in, in folding, residue
surface area in relation to)
L3 ANSWER 35 OF 46 CA COPYRIGHT 1996 ACS
AN 103:137451 CA
TI Molecular recognition. I. Automatic identification of topographic
surface features
AU Lee, Richard H.; ***Rose, George D.***
CS Milton S. Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA,
17033, USA
SO Biopolymers (1985), 24(8), 1613-27
CODEN: BIPMAA; ISSN: 0006-3525
DT Journal
LA English
CC 6-7 (General Biochemistry)
Section cross-reference(s): 9
AB The phenomenon of mol. recognition depends strongly on surface
complementarity between assocg. mol. units, analogous to the
assembly of a 3-dimensional jigsaw puzzle. The driving force for
assocn. is solvent entropy, which increases when protrusions of the
irregular surface of 1 subunit fit snugly into invaginations of the
other, squeezing out intervening water. To model this process, an
algorithm is presented that automatically finds the prominent topog.
surface features of rigid .alpha.-helixes in proteins of known
structure. When the algorithm was applied to 2 interacting helixes
from flavodoxin, only a small no. of such features were found, and
they accounted for the obsd. complementarity. By using this
algorithm, mol. docking can be reduced to a tractable problem by a
docking strategy based on exhaustive trial of combinations of
surface features.
ST mol recognition model algorithm; biopolymer surface feature analysis
algorithm; protein conformation surface interaction computer
algorithm; flavodoxin helix interaction mol recognition model
IT Algorithm
(for anal. of topog. surface features of proteins, mol.
recognition in relation to)
IT Computer application
(for protein topog. surface feature anal., mol. recognition in
relation to)
IT Flavodoxins
Proteins
RL: BIOL (Biological study)
(mol. recognition and docking in, algorithm for anal. of)
IT Biopolymers
RL: BIOL (Biological study)
(mol. recognition in, topog. surface feature anal. in relation
to)
IT Molecular association
(of proteins, topog. surface features in, algorithm for
identification of)
IT Conformation and Conformers
(.alpha.-helical, of proteins, in mol. recognition, algorithm for
anal. of mol. docking in relation to)
L3 ANSWER 36 OF 46 CA COPYRIGHT 1996 ACS
AN 101:73092 CA
TI Reverse turns in hydrophobic environments
AU Lacy, Jeffrey E.; Gierasch, Lila M.; Rockwell, Arlene L.; ***Rose,
George D.***
CS Dep. Chem., Univ. Delaware, Newark, DE, 19711, USA
SO Pept.: Struct. Funct., Proc. Am. Pept. Symp., 8th (1983), 781-4.
Editor(s): Hruby, Victor J.; Rich, Daniel H. Publisher: Pierce Chem.
Co., Rockford, Ill.
CODEN: 51KAAK
DT Conference
LA English
CC 34-3 (Amino Acids, Peptides, and Proteins)
Section cross-reference(s): 6, 22
AB The effect of a hydrophobic environment on the tendency of a
polypeptide chain to adopt reverse turn conformations was examd. by
(1) a computer search of globular proteins of known structure and
(2) NMR and CD spectral studies of synthetic peptides designed to
model hydrophobic turn sequences. A search of 22 proteins revealed
9 interior turns in which polar groups are H bonded either to water
or to other groups on the protein. The NMR and CD spectra of
R-X-D-Phe-D-Ala-L-Pro-NHMe [R = Me3CO2C, X = null (I); R = PhCH2O2C,
X = Pro (II)] solubilized in Na dodecyl sulfate (SDS) micelles
showed that I does not adopt a turn conformation, but the C-terminal
part of II adopts a .gamma. turn conformation. Me3CO2C-D-Tyr-Gly-L-
Ile-L-Leu-L-Gln-L-Pro-OH assumes a folded conformation in MeOH,
Me2SO, and aq. SDS solns.
ST conformation reverse turn peptide; hydrophobic soln conformation
peptide; hydrogen bond conformation peptide
IT Peptides, properties
RL: PRP (Properties)
(conformation of, in hydrophobic environments)
IT Hydrogen bond
(in peptides, reverse turn conformations in hydrophobic
environments in relation to)
IT Conformation and Conformers
(reverse-turn, of peptides in hydrophobic environment)
IT 84952-41-0 91302-80-6 91302-81-7
RL: PRP (Properties)
(conformation of, in hydrophobic environments)
L3 ANSWER 37 OF 46 CA COPYRIGHT 1996 ACS
AN 99:118083 CA
TI Interior turns in globular proteins
AU ***Rose, George D.*** ; Young, William B.; Gierasch, Lila M.
CS Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA, 17033,
USA
SO Nature (London) (1983), 304(5927), 654-7
CODEN: NATUAS; ISSN: 0028-0836
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB Reverse turns buried in the hydrophobic interior of globular
proteins were investigated in proteins of known sequence. In every
instance of a buried turn, .gtoreq.1 water mol. was found in a
H-bonded complex with main-chain atoms of the turn residues. Each
of the water mols. bound to an interior turn had .gtoreq.3 H-bonds.
Moreover, each polar group in these turns was H-bonded to either a
water mol. or to another interior polar group of the protein.
Instances of bifurcated H-bonds to these groups were also obsd. The
no. d. of individual water mols. H-bonded to an internal turn was
calcd. and showed that these water mols. were themselves buried deep
within the protein and not part of the bulk solvent. Thus,
constraints placed upon turns in a hydrophobic environment are
satisfied by incorporating water mols. into the structure as though
they were prosthetic groups.
ST conformation protein water hydrogen bond; water protein interior
turn stabilization
IT Hydrogen bond
(between protein polar residues and water, interior turn
stabilization in relation to)
IT Conformation and Conformers
(of globular proteins, interior turns in, hydrogen-bonded water
in)
IT Water of hydration
(protein interior turns stabilization by)
IT Proteins
RL: BIOL (Biological study)
(globular, interior turns in, hydrogen-bonded water in)
IT 9001-63-2 9001-84-7 9002-07-7 9002-08-8 9013-53-0
RL: BIOL (Biological study)
(interior turns in, hydrogen-bonded water in)
IT 9004-07-3
RL: BIOL (Biological study)
(.gamma., interior turns in, hydrogen-bonded water in)
L3 ANSWER 38 OF 46 CA COPYRIGHT 1996 ACS
AN 99:34751 CA
TI Hierarchic organization of globular proteins. A control study
AU Yuschok, Thomas J.; ***Rose, George D.***
CS Milton S. Hershey Med. Cent., Pennsylvania State Univ., Hershey, PA,
USA
SO Int. J. Pept. Protein Res. (1983), 21(5), 479-84
CODEN: IJPPC3; ISSN: 0367-8377
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB In previous work, globular proteins of known structure were shown to
be iteratively subdivisible into a hierarchy of disjunct,
contiguous-chain regions ranging from whole protein monomers down to
individual helixes and strands. The results of a similar anal.,
performed on a set of 1000 simulated chain folds generated by the
method of G. E. Schulz (1980), were reported. The organization of
these simulated proteins was similar to that of authentic mols.
This study strengthens earlier evidence suggesting that hierarchic
architecture is a ubiquitous attribute of protein chain folds.
ST globular protein conformation hierarchic organization
IT Conformation and Conformers
(of globular proteins, hierarchic organization in)
IT Proteins
RL: PRP (Properties)
(globular, conformation of, hierarchic organization in)
L3 ANSWER 39 OF 46 CA COPYRIGHT 1996 ACS
AN 95:128663 CA
TI Folding units in globular proteins
AU Lesk, Arthur M.; ***Rose, George D.***
CS Fairleigh Dickinson Univ., Teaneck, NJ, 07666, USA
SO Proc. Natl. Acad. Sci. U. S. A. (1981), 78(7), 4304-8
CODEN: PNASA6; ISSN: 0027-8424
DT Journal
LA English
CC 9-4 (Biochemical Methods)
Section cross-reference(s): 6, 34
AB A method is presented to identify all compact, contiguous-chain,
structural units in a globular protein from x-ray coordinates.
These units are then used to describe a complete set of hierarchic
folding pathways for the mol. The larger units are combinations of
smaller units, giving rise to a structural hierarchy ranging from
the whole protein monomer through supersecondary structures down to
individual helixes and strands. There is more than 1 way to
assemble the protein by self-assocn. of its compact units. However,
the no. of possible pathways is small enough to be exhaustively
explored by a computer program. The hierarchic organization of
compact units in protein mols. is consistent with a model for
folding by hierarchic condensation. In this model, neighboring
hydrophobic chain sites interact to form folding clusters, with
further stepwise cluster assocn. giving rise to a population of
folding intermediates.
ST computer application globular protein structure; globular protein
folding unit detn; x ray protein structure
IT Algorithm
Computer program
(for globular protein structure detn.)
IT Computer application
(in globular protein structure detn.)
IT Myoglobins
RL: PRP (Properties)
(structure of, computer program for study of folding units in)
IT Chains, chemical
(structure of, of proteins, computer program for study of folding
units in)
IT Proteins
RL: PRP (Properties)
(globular, structure of, computer program for study of folding
units in)
IT 9001-99-4
RL: PRP (Properties)
(structure of, computer program for study of folding units in)
L3 ANSWER 40 OF 46 CA COPYRIGHT 1996 ACS
AN 93:199540 CA
TI Hydrophobic basis of packing in globular proteins
AU ***Rose, George D.*** ; Roy, Siddhartha
CS Dep. Chem., Univ. Delaware, Newark, DE, 19711, USA
SO Proc. Natl. Acad. Sci. U. S. A. (1980), 77(8), 4643-7
CODEN: PNASA6; ISSN: 0027-8424
DT Journal
LA English
CC 6-3 (General Biochemistry)
Section cross-reference(s): 7
AB The self-assembly of globular proteins is often described as a
nucleation process in which the H bonding in segments of secondary
structure is the precondition for further folding. This concept is
unlikely because both the buried interior regions and the peptide
chain turns of the folded protein (i.e., inside and outside) are
predicted solely by the hydrophobicity of the residues, taken in
sequential order along the chain. The helixes and strands span the
protein, and this obsd. secondary structure is seen to coincide with
the regions predicted to be buried from hydrophobicity
considerations alone. Linear chain regions rich in hydrophobic
residues serve as small clusters that fold against each other, with
concomitant or even later fixation of secondary structure. A helix
or strand would arise in this folding process as 1 of a few
energetically favorable alternatives for a given cluster, followed
by a shift in the equil. between secondary structure conformers on
cluster assocn. The linear chain hydrophobicity alternates between
locally maximal and minimal values, and these extrema partition the
polypeptide chain into structural segments. This partitioning is
seen in the x-ray structure as isodirectional segments bracketed
between peptide chain turns, with the segments expressed most often
as helixes and strands. The segment interactions define the
geometry of the mol. interior and the chain turns describe the
predominant features of the mol. coastline. The segmentation of the
mol. by linear chain hydrophobicity imposes a major geometric
constraint on possible folding events.
ST folding protein hydrophobicity; conformation protein hydrophobicity;
enzyme folding hydrophobicity
IT Flavodoxins
Myoglobins
Parvalbumins
RL: BIOL (Biological study)
(folding of, hydrophobic domains in relation to)
IT Chains, chemical
(packing of, of proteins, hydrophobic domains in relation to)
IT Hydrophobicity
(protein packing in relation to)
IT Proteins
RL: BIOL (Biological study)
(globular, folding of, hydrophobic domains in relation to)
IT 9001-99-4
RL: BIOL (Biological study)
(A, folding of, hydrophobic domains in relation to)
IT 9001-63-2 9087-70-1
RL: BIOL (Biological study)
(folding of, hydrophobic domains in relation to)
L3 ANSWER 41 OF 46 CA COPYRIGHT 1996 ACS
AN 92:53654 CA
TI Hierarchic organization of domains in globular proteins
AU ***Rose, George D.***
CS Dep. Chem., Univ. Delaware, Newark, DE, 19711, USA
SO J. Mol. Biol. (1979), 134(3), 447-70
CODEN: JMOBAK; ISSN: 0022-2836
DT Journal
LA English
CC 6-3 (General Biochemistry)
Section cross-reference(s): 7
AB An automatic procedure was developed for the identification of
domains in globular proteins from x-ray-elucidated coordinates.
Using this tool, domains were shown to be iteratively decomposable
into subdomains, leading to a hierarchic mol. architecture. There
is no convenient geometry that will fully characterize the atom by
atom interdigitation at an interface between domains, and the
strategy adopted here was devised to reduce this unwieldy
3-dimensional problem to a closely approximating companion anal. in
a plane. These anal. derived domain choices can be used
subsequently to construct computer-generated, space-filling,
color-coded views of the domains; and when this is done, the derived
domains are seen to be completely resolved. The no. of domains in a
protein is a math. well-behaved function of the chain length,
lending support to the supposition that the domains are an implicit
structural consequence of the folding process. A spectrum of
domains ranging in size from whole protein monomers to the
individual units of secondary structure was apparent in each of 22
proteins analyzed. The hierarchic organization of structural
domains is evidence in favor of an underlying protein folding
process that proceeds by hierarchic condensation. In this highly
constrained model, every pathway leading to the native state can be
described by a tree of local folding interactions.
ST protein domain hierarchic organization; enzyme domain hierarchic
organization
IT Chains, chemical
(conformation of, of globular proteins, hierarchic organization
of domains in)
IT Flavodoxins
Myogens
Rubredoxins
RL: PRP (Properties)
(domain structure of)
IT Proteins
RL: PRP (Properties)
(globular, domains in, hierarchic organization of)
IT Proteins
RL: PRP (Properties)
(iron-contg., high-potential, domain structure of)
IT 9001-03-0
RL: BIOL (Biological study)
(B, domain structure of)
IT 9001-50-7 9001-51-8 9001-60-9 9001-63-2 9001-73-4
9001-99-4 9004-07-3 9007-43-6, properties 9014-01-1
9031-72-5 9032-62-6 9035-39-6 9054-89-1 9087-70-1
11028-71-0 11075-17-5
RL: PRP (Properties)
(domain structure of)
L3 ANSWER 42 OF 46 CA COPYRIGHT 1996 ACS
AN 89:55012 CA
TI Prediction of chain turns in globular proteins on a hydrophobic
basis
AU ***Rose, George D.***
CS Dep. Chem., Univ. Delaware, Newark, Del., USA
SO Nature (London) (1978), 272(5654), 586-90
CODEN: NATUAS; ISSN: 0028-0836
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB The hypothesis is proposed that peptide chain turns in globular
proteins occur at those sites in the polypeptide chain where the
hydrophobicity is at a local min. A method was presented for
locating the turns specified by this hypothesis by examg. the amino
acid sequence and amino acid hydrophobicities. A favorable
comparison of measured and predicted turns for adenyl kinase is
made. In addn., the hypothesis accounts for the hydrophobic core of
proteins.
ST peptide chain turn protein hypothesis; protein hydrophobic structure
hypothesis
IT Chains, chemical
(conformation of, of globular proteins, prediction of turns in)
IT Amino acids, properties
RL: PRP (Properties)
(hydrophobicity of side-chains of, prediction of chain turns in
globular proteins in relation to)
IT Hydrophobicity
(of amino acid side chains, prediction of chain turns in globular
proteins in relation to)
IT Proteins
RL: PRP (Properties)
(globular, conformation of, prediction of chain turns in)
IT 9013-02-9
RL: PRP (Properties)
(conformation of, prediction of chain turns in)
L3 ANSWER 43 OF 46 CA COPYRIGHT 1996 ACS
AN 88:84753 CA
TI The number of turns in globular proteins
AU ***Rose, George D.*** ; Wetlaufer, Donald B.
CS Dep. Chem., UNiv. Delaware, Newark, Del., USA
SO Nature (London) (1977), 268(5622), 769-70
CODEN: NATUAS
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB Two possible models explaining the turn formation in peptide chains
of globular proteins emerged after examn. of the no. of turns in 21
proteins ranging in size from 53-450 amino acid residues. The no.
of turns was a linear function of the no. of amino acid residues in
the protein. A sequence anal. of myoglobin detd. sequence dependent
sites still discernible after folding, which was interpreted as
partitioning the protein into its structural segments and turns by
local sequences of amino acids. The interpretation was consistent
with the model of R. (1976).
ST protein globular peptide turn; myoglobin peptide turn
IT Peptides, properties
RL: PRP (Properties)
(chain folding of, in globular proteins, calcn. of)
IT Chains, chemical
(folding of, in globular proteins, model of)
IT Proteins
RL: BIOL (Biological study)
(globular, turns in, no. of, model for)
L3 ANSWER 44 OF 46 CA COPYRIGHT 1996 ACS
AN 87:97611 CA
TI A new algorithm for finding the peptide chain turns in a globular
protein
AU ***Rose, George D.*** ; Seltzer, Jack P.
CS Dep. Chem., Univ. Delaware, Newark, Del., USA
SO J. Mol. Biol. (1977), 113(1), 153-64
CODEN: JMOBAK
DT Journal
LA English
CC 6-3 (General Biochemistry)
Section cross-reference(s): 7
AB An algorithm is presented to identify peptide chain turns from
x-ray-elucidated coordinate data. Chain turns are those regions in
a globular protein where the backbone is folded back upon itself.
The algorithm presented here uses only the .alpha.C coordinates for
every residue in the protein. No other information is required;
notions about H bonding at these loci are irrelevant to the
geometric nature of the argument. The algorithm provides an
objective criterion for the recognition of turns as strictly
structural components in proteins. The algorithm is used to find
the turns in a test set of proteins. Results of this application
are in excellent agreement with visual turn identification from
phys. models.
ST protein chain folding algorithm; enzyme chain folding algorithm
IT Enzymes
Flavodoxins
Proteins
RL: PRP (Properties)
(conformation of, folding in, algorithm for)
IT Chains, chemical
(folding of, of proteins, algorithm for)
IT Algorithm
(for chain folding, in proteins)
IT 9001-99-4
RL: BIOL (Biological study)
(S, conformation of, folding in, algorithm for)
IT 9001-63-2 9014-01-1 9026-81-7 9035-81-8
RL: PRP (Properties)
(conformation of, folding in, algorithm for)
L3 ANSWER 45 OF 46 CA COPYRIGHT 1996 ACS
AN 86:12895 CA
TI Orientation of structural segments in globular proteins
AU Wetlaufer, Donald B.; ***Rose, George D.*** ; Taaffe, Laurence
CS Med. Sch., Univ. Minnesota, Minneapolis, Minn., USA
SO Biochemistry (1976), 15(23), 5154-7
CODEN: BICHAW
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB Twelve globular proteins were examd. to test whether structural
segments are oriented at random. Structural segments are defined as
the primary sequence of linear chain neighbors bounded by
consecutive peptide chain turns. A structural segment can be well
approximated by a straight-line segment. Each protein in the test
set was exhaustively partitioned into its constituent structural
segments. A method is presented for comparing pairwise intersegment
orientations. Within a protein, 3-dimensionally close segments
exhibit a pronounced tendency toward parallel orientation, whereas
distant segments are randomly oriented. Some conclusions are
presented relating to the general problem of segment packing in
globular proteins.
ST protein structure segment orientation
IT Flavodoxins
RL: PRP (Properties)
(structural segment orientation in)
IT Proteins
RL: PRP (Properties)
(globular, structural segment orientation in)
IT 9001-60-9 9001-63-2
RL: PRP (Properties)
(structural segment orientation in)
L3 ANSWER 46 OF 46 CA COPYRIGHT 1996 ACS
AN 84:131764 CA
TI A testable model for protein folding
AU ***Rose, George D.*** ; Winters, Ronald H.; Wetlaufer, Donald B.
CS Comput. Cent., Oregon State Univ., Corvallis, Oreg., USA
SO FEBS Lett. (1976), 63(1), 10-16
CODEN: FEBLAL
DT Journal
LA English
CC 6-3 (General Biochemistry)
AB A testable, biphasic model for protein folding is formulated. In
this model, linearly short and medium range interactions dominate
early folding, causing the chain to assume independently nucleated
modules of persisting structure termed Local Independently Nucleated
Continuous segments (LINCs). In a later stage of folding, the LINCs
fold relative to each other, and it is only at this time that the
protein assumes its characteristic interior and exterior and its
overall globular structure. In the perspective of this model, a
computational approach is outlined, requiring 1st a systematic
examn. of steric and energetic constraints that can be calcd. with
some confidence by accepted means. The sterically allowed
conformation was calcd. for: (1) a post-helical residue situated at
the C-terminal end of a backbone-only helix, (2) various side-chains
of an intrahelical residue, and (3) the constraints imposed on
lysine and arginine side-chains if some accounting is made for
hydration of the resp. cationic side-chain moieties. Substantial
steric constraints were engendered in all 3 cases.
ST protein folding model; conformation protein model
IT Proteins
RL: BIOL (Biological study)
(folding of, model for)
IT Chains, chemical
(folding of, of proteins, model for)
=> s expand rose g/au
E1 1 ROSE FRIEDRICH W/AU
E2 20 ROSE FRITZ/AU
E3 55 --> ROSE G/AU
E4 21 ROSE G A/AU
E5 27 ROSE G ALAN/AU
E6 6 ROSE G D/AU
E7 1 ROSE G E/AU
E8 2 ROSE G G/AU
E9 3 ROSE G L/AU
E10 5 ROSE G M/AU
E11 9 ROSE G P/AU
E12 3 ROSE G R/AU
=> s e3 and e or e6
55 "ROSE G"/AU
6 "ROSE G D"/AU
L4 61 "ROSE G"/AU OR "ROSE G D"/AU
=> display l4 1-61 all
L4 ANSWER 1 OF 61 CA COPYRIGHT 1996 ACS
AN 124:102177 CA
TI Fast deposition of polycrystalline silicon films by hot-wire CVD
AU Middya, A. R.; Lloret, A.; Perrin, J.; Huc, J.; Moncel, J. L.;
Parey, J. Y.; ***Rose, G.***
CS Lab. Phys. Interfaces Couches Minces, Ecole Polytech., Palaiseau,
F-91128, Fr.
SO Mater. Res. Soc. Symp. Proc. (1995), 377(Amorphous Silicon
Technology-1995), 119-24
CODEN: MRSPDH; ISSN: 0272-9172
DT Journal
LA English
CC 75-1 (Crystallography and Liquid Crystals)
AB Polycryst. Si thin films were deposited at fast growth rates (50
.ANG./s) by hot-wire CVD (HW-CVD) from SiH4/H2 gas mixts. at low
substrate temp. (400-500.degree.). The surface morphol. of these
films consists of 0.5-2.0 .mu.m dendritic grains as seen by electron
microscopy. The films have a columnar morphol. with grains starting
from the substrate either on glass or c-Si. Even the 150 nm thick
initial layer is polycryst. The preferential cryst. orientation of
the poly-Si film is apparently not governed by the radiative source
but strongly depends on the type and orientation of the substrate.
A strong H diln. (>90%) of silane is essential to obtain poly-Si
films with optimal cryst. structure.
ST fast deposition polycryst silicon film CVD
IT Vapor deposition processes
(hot-wire; of polycryst. silicon films)
IT Crystallization
(of silicon films by fast hot-wire CVD)
IT Surface structure
(of silicon polycryst. films grown by hot-wire CVD)
IT 7440-21-3, Silicon, processes
RL: PEP (Physical, engineering or chemical process); PROC (Process)
(fast deposition of polycryst. silicon films by hot-wire CVD)
L4 ANSWER 2 OF 61 CA COPYRIGHT 1996 ACS
AN 121:150497 CA
TI The first genetic marker detected in the promoter region of the
thyroid peroxidase gene by single-strand conformational polymorphism
analysis
AU ***Rose, G.*** ; De Luca, M.; Leone, O.; Falcone, E.; Chimienti,
G.; Pepe, G.; Giacchetto, C.; De Benedictis, G.
CS Cell Biol. Dep., Univ. Calabria, Rende, Italy
SO Hum. Mutat. (1993), 2(5), 418-19
CODEN: HUMUE3; ISSN: 1059-7794
DT Journal
LA English
CC 3-6 (Biochemical Genetics)
Section cross-reference(s): 13
AB PCR-single-strand conformational polymorphism (SSCP) anal. revealed
2 codominant alleles, TPO*P1 and TPO*P2. Family anal. confirmed the
Mendelian inheritance of the polymorphism. The *P1 and *P2 allelic
frequencies were 0.567 and 0.433, esp., and the genotypic
distribution was in Hardy-Weinberg equil. DNA sequencing of the
polymorphic fragment performed on PCR products from 3 different
phenotypes indicated that the *P1 and *P2 alleles can be regarded as
haplotypes. Thus, PCR-SSCP detected the 1st genetic marker in a DNA
region crucial for TPO gene expression.
ST thyroid peroxidase gene promoter marker
IT Gene, animal
RL: BIOL (Biological study)
(TPO, for thyroid peroxidase, genetic marker in promoter region
of human)
IT Genetic element
RL: BIOL (Biological study)
(promoter, genetic marker in, of human thyroid peroxidase gene)
IT 9031-28-1, Thyroid peroxidase
RL: BIOL (Biological study)
(gene for, genetic marker in promoter region of human)
L4 ANSWER 3 OF 61 CA COPYRIGHT 1996 ACS
AN 120:155442 CA
TI Rapid identification of VNTR alleles of the human thyroid peroxidase
gene by PCR: A study in a population sample from south Italy
AU ***Rose, G.*** ; De Luca, M.; Falcone, E.; Giacchetto, C.; De
Benedictis, G.
CS Cell Biol. Dep., Univ. Calabria, Calabria, Italy
SO Genomics (1993), 17(3), 796-8
CODEN: GNMCEP; ISSN: 0888-7543
DT Journal
LA English
CC 3-3 (Biochemical Genetics)
Section cross-reference(s): 13
AB VNTR alleles of the human thyroid peroxidase gene were detd. by PCR.
Frequencies of alleles in a population sample from south Italy are
reported. This VNTR polymorphism maybe useful in forensic and
genetic studies.
ST human thyroid peroxidase gene polymorphism
IT Genetic polymorphism
(VNTR, of human thyroid peroxidase gene)
IT Polymerase chain reaction
(for identification of VNTR alleles of human thyroid peroxidase
gene)
IT Gene, animal
RL: BIOL (Biological study)
(for thyroid peroxidase of human, PCR detection of VNTR
polymorphic alleles of)
IT 153574-61-9 153574-62-0
RL: PRP (Properties)
(as DNA primer in polymerase chain reaction, for identification
of VNTR alleles of human thyroid peroxidase gene)
IT 9031-28-1, Thyroid peroxidase
RL: PRP (Properties)
(human gene for, PCR detection of VNTR polymorphic alleles of)
L4 ANSWER 4 OF 61 CA COPYRIGHT 1996 ACS
AN 119:215042 CA
TI Two-fluid interpretation of the conductivity of clean BCS
superconductor
AU Berlinsky, A. John; Kallin, C.; ***Rose, G.*** ; Shi, A. C.
CS Inst. Mater. Res., McMaster Univ., Hamilton, ON, L8S 4M1, Can.
SO Phys. Rev. B: Condens. Matter (1993), 48(6), 4074-9
CODEN: PRBMDO; ISSN: 0163-1829
DT Journal
LA English
CC 76-4 (Electric Phenomena)
AB The temp. and frequency dependence of the microwave and optical
cond. are studied for a BCS superconductor with weak elastic
scattering [1/.tau.<2.DELTA.(0), where .tau. is the scattering time
and .DELTA.(T) is the BCS energy gap]. The results are interpreted
in terms of a two-fluid model in which the combined oscillator
strength of the .delta. function at the origin and the thermally
excited free-carrier cond. is found to be only weakly temp.
dependent. The low-frequency cond. is a function of .omega..tau.,
in the clean limit, with a characteristic logarithmic divergence at
.omega.=0. The frequency dependence of the microwave surface
resistance is discussed and comparison is made to the recent exptl.
results of Bonn, Hardy, and co-worker on YBa2Cu3O7-.delta. single
crystals.
ST cond BCS superconductor two fluid model
IT Superconductors
(two-fluid model of BCS)
IT Superconductivity
(two-fluid model of, of BCS superconductors)
IT Electric resistance
(surface, microwave-frequency-dependent, of BCS superconductors,
two-fluid model and)
L4 ANSWER 5 OF 61 CA COPYRIGHT 1996 ACS
AN 116:208951 CA
TI Acyl-RFLP in intron 8 of hTPO gene
AU ***Rose, G.*** ; Leone, O.; Giacchetto, C.; De Benedictis, G.
CS Cell Biol. Dep., Univ. Calabria, Rende, Italy
SO Nucleic Acids Res. (1992), 20(5), 1162
CODEN: NARHAD; ISSN: 0305-1048
DT Journal
LA English
CC 3-3 (Biochemical Genetics)
Section cross-reference(s): 13
AB Two primers TPO-8a and TPO-8b were used to amplify a 755bp long
fragment of the TPO gene including exon 8 plus 18bp upstream and
219bp downstream of this exon. After PCR amplification the products
were digested by AcyI restriction endonuclease and electrophoresed
on 6% Nu Sieve Agarose. The published sequence (Kimura et al.,
1987) reports five AcyI sites on this target. The two bands due to
the AcyI site located 114bp downstream of exon 8 resulted clearly
polymorphic: the 64bp and 59bp long fragments (G1) were replaced in
some examples by one band of 123bp (G2) (loss of AcyI site). The
other expected bands were present in all the samples. Frequencies
were estd. in 49 unrelated Caucasians. Co-dominant segregation
shown in one pedigree (18 individuals with 8 significant meioses).
ST gene TPO intron polymorphism human
IT Proteins, specific or class
RL: BIOL (Biological study)
(gene TPO, polymorphism in intron 8 of gene for, of human)
IT Gene, animal
RL: BIOL (Biological study)
(TPO, of human, polymorphism in intron 8 of)
IT Genetic polymorphism
(AcyI, in gene TPO intron 8, of human)
IT Genetic element
RL: BIOL (Biological study)
(intron, 8, of gene TPO of human, polymorphism in)
L4 ANSWER 6 OF 61 CA COPYRIGHT 1996 ACS
AN 115:166261 CA
TI Characterization of composite membranes by their nonequilibrium
thermodynamic transport parameters
AU Forgach, D. J.; ***Rose, G. D.*** ; Luteneske, N. E.
CS Cent. Res., Dow Chem. Co., Midland, MI, 48674, USA
SO Desalination (1991), 80(2-3), 275-92
CODEN: DSLNAH; ISSN: 0011-9164
DT Journal
LA English
CC 61-5 (Water)
Section cross-reference(s): 38
AB Composite reverse osmosis membranes were prepd. by interfacially
polymg. arom. polyamide discriminating layers on the inside surface
of microporous polyethersulfone hollow fibers and on the surface of
flat sheet polysulfone ultrafilters. The salt rejection and flux of
these membranes were measured at various feed pressures. From these
measurements, the membrane reflection coeffs., salt permeances and
hydraulic permeances were estd. Neither the polysulfone
ultrafilters nor the microporous polyethersulfone hollow fibers
possessed any inherent salt rejecting capability. Both had a
hydraulic permeance .gtoreq.2 orders of magnitude greater than that
of the resp. composite membranes. Consequently, it was concluded
that the estd. transport parameters for both composite membranes
were characteristic exclusively of their polyamide discriminating
layers. Comparison of these transport parameters generated insight
into structural and functional aspects of the membrane that can not
be visualized by SEM.
ST composite membrane reverse osmosis water; thermodn transport
parameter composite membrane
IT Polyamides, uses and miscellaneous
RL: OCCU (Occurrence)
(hollow fiber reverse osmosis membrane from polyethersulfones
and, nonequil. thermodn. transport parameters for, water purifn.
in relation to)
IT Permeability and Permeation
(of salts through composite membranes, water purifn. in relation
to)
IT Polysulfones, uses and miscellaneous
RL: USES (Uses)
(polyether-, hollow fiber reverse osmosis membranes from arom.
polyamides and,)
IT Polyethers, uses and miscellaneous
RL: USES (Uses)
(polysulfone-, hollow fiber reverse osmosis membranes from arom.
polyamides and,)
IT Water purification
(reverse osmosis, composite membranes for, nonequil. thermodn.
transport parameters for)
IT 83044-99-9, m-Phenylene diamine-trimesoyl chloride copolymer
RL: OCCU (Occurrence)
(hollow fiber reverse osmosis membrane from polyethersulfones
and, nonequil. thermodn. transport parameters for, water purifn.
in relation to)
IT 7732-18-5
RL: AMX (Analytical matrix); ANST (Analytical study)
(permeability and Permeation, of salts through composite
membranes, water purifn. in relation to)
L4 ANSWER 7 OF 61 CA COPYRIGHT 1996 ACS
AN 115:165533 CA
TI Urea injection nitrogen oxide (NOx) removal in European coal-fired
boilers and MSW incineration plants
AU Jones, D. G.; Negrea, Stefan; Lautenschlager, G.; ***Rose, G.***
; Smith, R. A.; Shiomoto, G. H.
CS Noell-KRC, Visalia, CA, USA
SO Proc. - A&WMA Annu. Meet. (1990), 83rd(Vol. 2), 90/32.3, 14 pp.
CODEN: PAMEE5; ISSN: 1052-6102
DT Journal
LA English
CC 59-4 (Air Pollution and Industrial Hygiene)
Section cross-reference(s): 51, 60
AB Data from 2 European applications of an advanced urea injection
technol. show 50-70% NOx removal from waste incineration flue gases
with relatively low levels of NH3 slip. In both cases, proprietary
injection nozzle systems were used to provide mixing and
distribution of small amts. of urea into large vols. of crossflowing
flue gas. The data also show high levels of DeNOx performance
achieved using urea injection at flue gas temps. .apprx.1600-1900 F.
Com.-available urea can be used in a water mixt., and no other
chems. or additives are necessary. Relatively high levels of NOx
removal can be obtained using urea injection and properly-designed
injection nozzle systems in large-scale boilers.
ST nitrogen oxide removal incineration flue gas; waste incineration gas
denitration urea injection; flue gas denitration urea injection
IT Incineration
(flue gases from, nitrogen oxide removal from, advanced urea
injection DeNOx process for)
IT Boilers
(coal-fired, flue gases from, nitrogen oxide removal from,
advanced urea injection DeNOx process for)
IT Flue gases
(incinerator, nitrogen oxide removal from, advanced urea
injection DeNOx process for)
IT 57-13-6, Urea, uses and miscellaneous
RL: USES (Uses)
(nitrogen oxide removal by injection of, from incinerator flue
gases, advanced DeNOx method for)
IT 7664-41-7, Ammonia, uses and miscellaneous
RL: USES (Uses)
(release and control of, in incinerator flue gas denitration by
advanced urea injection DeNOx process)
IT 11104-93-1, Nitrogen oxide, uses and miscellaneous
RL: REM (Removal or disposal); PROC (Process)
(removal of, from incinerator flue gases, advanced urea injection
technol. for)
L4 ANSWER 8 OF 61 CA COPYRIGHT 1996 ACS
AN 115:128994 CA
TI AcyI-RFLP identified on an amplified region of the TPO gene
AU ***Rose, G.*** ; Giacchetto, C.; De Benedictis, G.
CS Cell Biol. Dep., Univ. Calabria, Rende, Italy
SO Nucleic Acids Res. (1991), 19(14), 4021
CODEN: NARHAD; ISSN: 0305-1048
DT Journal
LA English
CC 3-3 (Biochemical Genetics)
Section cross-reference(s): 13
AB Polymerase chain reaction primers were designed to detect an AcyI
restriction fragment length polymorphism (RFLP) of the human thyroid
peroxidase gene located on chromosome 2pter-p12. An inspection of
the ref. sequence showed that an A .fwdarw. C mutation 212 bp
upstream from exon 10 was the origin of the AcyI restriction site
(Allele - : GGAGCC .fwdarw. Allele + : GGCGCC). The frequencies of
allele + and allele - were 0.66, and 0.34, resp., in 64 unrelated
caucasians. Codominant segregation was obsd. in 6 families.
ST thyroid peroxidase gene AcyI RFLP human; polymorphism thyroid
peroxidase gene human
IT Gene and Genetic element, animal
RL: BIOL (Biological study)
(for thyroid peroxidase, of human, restriction fragment length
polymorphism in)
IT Chromosome
(human 2, thyroid peroxidase gene on, restriction fragment length
polymorphism in)
IT Genetic polymorphism
(restriction fragment length, in thyroid peroxidase gene of
human)
IT 9031-28-1, Thyroid peroxidase
RL: PRP (Properties)
(gene for human, AcyI restriction fragment length polymorphism
in)
L4 ANSWER 9 OF 61 CA COPYRIGHT 1996 ACS
AN 114:252992 CA
TI Blood lead concentration, renal function, and blood pressure in
London civil servants
AU Staessen, J.; Yeoman, W. B.; Fletcher, A. E.; Markowe, H. L. J.;
Marmot, M. G.; ***Rose, G.*** ; Semmence, A.; Shipley, M. J.;
Bulpitt, C. J.
CS R. Postgrad. Med. Sch., Hammersmith Hosp., London, W12 0HS, UK
SO Br. J. Ind. Med. (1990), 47(7), 442-7
CODEN: BJIMAG; ISSN: 0007-1072
DT Journal
LA English
CC 59-2 (Air Pollution and Industrial Hygiene)
Section cross-reference(s): 4
AB Blood Pb concn., measured in 398 male and 133 female London civil
servants not subject to industrial exposure to heavy metals, ranged
from 0.20 to 1.70 .mu.mol/L with a geometric mean concn. of 0.58
.mu.mol/L in men and 0.46 .mu.mol/L in women (p <0.001). In women
blood Pb concn. increased with age. In both sexes blood Pb concn.
was pos. correlated with the no. of cigarets smoked a day, with the
reported no. of alc. beverages consumed a day, and with serum
.gamma.-glutamyltranspeptidase. In men 14% of the variance of blood
Pb concn. was explained by the significant and independent
contributions of smoking and alc. intake and in women 16% by age,
smoking, and alc. consumption. In men serum creatinine concn.
increased by 0.6 .mu.mol/L for each 25% increment in blood Pb concn.
In conclusion, in subjects not exposed to heavy metals at work,
gender, age, smoking, and alc. intake are determinants of blood Pb
concn. At a low level of exposure, Pb accumulation may slightly
impair renal function, whereas blood pressure does not seem to be
importantly influenced. Alternatively, a slight impairment of renal
function may give rise to an increase in blood Pb concn.
ST blood lead nonoccupational London England; tobacco smoking blood
lead England; alc consumption blood lead England; creatinine blood
lead blood England; kidney function lead blood England
IT Blood pressure
Tobacco smoke and smoking
(blood lead levels in relation to, in nonoccupationally exposed
men and women in London, England)
IT Environmental pollution
(by lead, blood lead levels in relation to, determinants of, in
nonoccupationally exposed men and women in London, England)
IT Alcoholic beverages
(consumption of, blood lead levels in relation to, in
nonoccupationally exposed men and women in London, England)
IT Blood serum
(creatinine in, blood lead levels in relation to, in
nonoccupationally exposed men and women in London, England)
IT Blood
(lead concns. in, determinants of, in nonoccupationally exposed
men and women in London, England)
IT 64-17-5
RL: OCCU (Occurrence)
(alcoholic beverages, consumption of, blood lead levels in
relation to, in nonoccupationally exposed men and women in
London, England)
IT 64-17-5, Ethanol, biological studies
RL: BIOL (Biological study)
(consumption of, blood lead levels in relation to, in
nonoccupationally exposed men and women in London, England)
IT 60-27-5, Creatinine
RL: ADV (Adverse effect, including toxicity); BIOL (Biological
study)
(in blood serum, blood lead levels in relation to, in
nonoccupationally exposured men and women in London, England)
IT 7439-92-1, Lead, biological studies
RL: BIOL (Biological study)
(in blood, of nonoccupationally exposed men and women,
determinants of, in London, England)
L4 ANSWER 10 OF 61 CA COPYRIGHT 1996 ACS
AN 114:40646 CA
TI Post-translational polymorphism of human IgA identified by
immunoisoelectrofocusing
AU De Benedictis, G.; ***Rose, G.*** ; Brancati, C.
CS Dep. Cell Biol., Univ. Calabria, Arcavacata, 87030, Italy
SO J. Immunogenet. (1990), 17(1-2), 43-50
CODEN: JIMGAV; ISSN: 0305-1811
DT Journal
LA English
CC 15-3 (Immunochemistry)
AB Immunoisoelectrofocusing (IIEF) reveals a microheterogeneity of
human serum IgA controlled by an autosomal polymorphic gene, termed
S. The microheterogeneity disappears when sialic acid is removed
from serum glycoproteins by neuraminidase treatment. Gene S might
encode a sialyltransferase which attaches sialic acid at the outer
prosthetic chain of IgA.
ST IgA polymorphism gene S human
IT Genetic polymorphism
(in IgA oligosaccharide microheterogeneity, in humans, gene S in
relation to)
IT Sialic acids
RL: BIOL (Biological study)
(in IgA oligosaccharide polymorphism, in humans, gene S in
relation to)
IT Immunoglobulins
RL: BIOL (Biological study)
(A, oligosaccharide polymorphism of human, sialic acid and gene S
in)
IT Oligosaccharides
RL: BIOL (Biological study)
(sialo-, of IgA, polymorphism of human, gene S in)
IT Gene and Genetic element, animal
RL: BIOL (Biological study)
(S, in IgA oligosaccharide polymorphism, in humans)
IT 9075-81-4, Sialyltransferase
RL: BIOL (Biological study)
(in IgA oligosaccharide polymorphism in human)
L4 ANSWER 11 OF 61 CA COPYRIGHT 1996 ACS
AN 114:37352 CA
TI Neurobehavioral and sensory irritant effects of controlled exposure
to a complex mixture of volatile organic compounds
AU Otto, D.; Molhave, L.; ***Rose, G.*** ; Hudnell, H. K.; House, D.
CS Health Eff. Res. Lab., U. S. Environ. Prot. Agency, Research
Triangle Park, NC, 27711, USA
SO Neurotoxicol. Teratol. (1990), 12(6), 649-52
CODEN: NETEEC; ISSN: 0892-0362
DT Journal
LA English
CC 4-3 (Toxicology)
Section cross-reference(s): 59
AB Subjective reactions of discomfort, impaired air quality, irritation
of mucosal membranes, and impaired memory have been reported in
chem. sensitive subjects during exposure to volatile org. compds.
(VOCs) found in new buildings. Sixty-six normal healthy male
subjects aged 18-39 were exposed for 2.75 h to a complex VOC mixt.
at 0 and 25 mg/m3. Each subject completed control and exposure
sessions at 1-wk intervals in counterbalanced order. Measurements
included comfort ratings of eye, nose and throat irritation, symptom
questionnaire and computerized behavioral tests. Subjects found the
odor of VOCs unpleasantly strong and reported that VOC exposure
degraded air quality, increased headache, and produced general
discomfort. VOC exposure did not affect performance on any
behavioral tests.
ST volatile org compd behavior; air pollution indoor behavior irritant
effect
IT Volatile substances
(org., irritant effect of, neurobehavioral response to, in
humans)
IT Behavior
Learning
Memory, biological
Mental activity
(volatile org. compds. effect on, in humans)
IT Air pollution
(indoor, from volatile org. compds., irritant effect of,
neurobehavioral response to, in humans)
IT 66-25-1, n-Hexanal 67-63-0, Isopropanol, biological studies
71-36-3, n-Butanol, biological studies 75-34-3, 1,1-Dichloroethane
78-93-3, 2-Butanone, biological studies 80-56-8, .alpha.-Pinene
95-63-6, 1,2,4-Trimethylbenzene 100-41-4, Ethylbenzene, biological
studies 103-65-1, n-Propylbenzene 106-42-3, p-Xylene, biological
studies 108-10-1, 4-Methyl-2-pentanone 110-54-3, n-Hexane,
biological studies 110-62-3, n-Pentanal 110-82-7, Cyclohexane,
biological studies 111-15-9 111-66-0, 1-Octene 111-84-2,
n-Nonane 123-86-4, n-Butylacetate 124-18-5, n-Decane 872-05-9,
1-Decene 1120-21-4, n-Undecane
RL: PRP (Properties)
(irritant effect of, neurobehavioral response to, in humans)
L4 ANSWER 12 OF 61 CA COPYRIGHT 1996 ACS
AN 114:22860 CA
TI Diagnostic nitrogen concentrations for cabbages grown in sand
culture
AU Huett, D. O.; ***Rose, G.***
CS Trop. Fruit Res. Stn., NSW Agric. Fish., Alstonville, 2477,
Australia
SO Aust. J. Exp. Agric. (1989), 29(6), 883-92
CODEN: AJEAEL; ISSN: 0816-1089
DT Journal
LA English
CC 19-1 (Fertilizers, Soils, and Plant Nutrition)
AB The cabbage cv. Rampo was grown in sand culture with 5 nitrogen (N)
levels, between 2 and 43 mmol/L, applied as nitrate each day in a
complete nutrient soln. The youngest fully opened leaf (YFOL),
which became the wrapper leaf at heading, the youngest fully
expanded leaf (YFEL) and the oldest green leaf (OL) were harvested
at a min. of 2-wk intervals over a 12-wk growth period. Std. lab.
leaf total N and nitrate-N detns. and rapid petiole sap nitrate-N
detns. were conducted on YFOL, YFEL, and OL. Total N was also detd.
in bulked leaves. The relationship between growth rate relative to
the max. at each sampling time and leaf N concn. was used to derive
diagnostic petiole sap nitrate-N, leaf nitrate-N, and total N in
YFOL, YFEL, and OL and bulked leaf total N concns. Crit. concn.
corresponded to 90% max. growth rate and adequate concn.
corresponded to 91-100% max. growth rate. Petiole sap nitrate-N
concn., which can be measured rapidly in the field, and leaf
nitrate-N concn. were very responsive to N application where pos.
growth responses were recorded. Crit. N concns. are presented for
all leaves at most sampling times throughout the growth period.
Crit. total N concns. in YFOL, YFEL, and bulked leaves were higher
during the pre-heading growth stage (weeks 2-6) than the
post-heading growth stage (weeks 8-12). Crit. N concns. were
inconsistent over the growth period and it was not possible to
present single values to represent the full growth period, with 2
exceptions. A crit. petiole sap nitrate-N concn. for OL of 3.0 g/L
can be recommended for the full growth period because it represents
a percentage of max. growth rate range of 88-95%. Similarly, for
YFEL, a crit. total N concn. of 4.10% pre-heading (range 4.10-4.38%)
represents a percentage max. growth rate range of 62-90% and a
post-heading crit. total N concn. of 3.10% (range 3.10-3.50%)
represents a percentage max. growth rate range of 76-90%. The
concns. of potassium, phosphorus, calcium, magnesium and sulfur in
YFOL, YFEL, OL, and bulked leaf corresponding to N treatments
producing max. growth rates are also presented.
ST nitrogen cabbage leaf nutritional status detn
IT Cabbage
(nitrogen concn. in leaves of, nutritional status detn. by)
IT Plant nutrition
(nitrogen, status of, of cabbage, leaf anal. in detn. of)
IT 7439-95-4, Magnesium, biological studies 7440-09-7, Potassium,
biological studies 7440-70-2, Calcium, biological studies
7704-34-9, Sulfur, biological studies 7723-14-0, Phosphorus,
biological studies
RL: BIOL (Biological study)
(in cabbage leaves, nitrogen treatments and nutritional status in
relation to)
IT 7727-37-9, Nitrogen, biological studies 14797-55-8, Nitrate,
biological studies
RL: BIOL (Biological study)
(in cabbage leaves, nutritional status in relation to)
IT 7727-37-9
RL: BIOL (Biological study)
(plant nutrition, nitrogen, status of, of cabbage, leaf anal. in
detn. of)
L4 ANSWER 13 OF 61 CA COPYRIGHT 1996 ACS
AN 110:215236 CA
TI Drag reduction and rheological properties of cationic viscoelastic
surfactant formulations
AU ***Rose, G. D.*** ; Foster, K. L.
CS Interfacial Sci. Funct. Polym. Lab., Dow Chem. Co., Midland, MI,
48674, USA
SO J. Non-Newtonian Fluid Mech. (1989), 31(1), 59-85
CODEN: JNFMDI; ISSN: 0377-0257
DT Journal
LA English
CC 46-4 (Surface Active Agents and Detergents)
AB The characteristic times obtained on an aq. soln. of 0.2 wt.%
cetyltrimethylammonium salicylate (I) plus 0.2 wt.% Na salicylate
(II) using steady shearing measurements increased with temp., in
agreement with drag redn. activity (d). The effect of temp. on the
crossover frequency also correlated well with d for 0.2 wt.% I aq.
solns. at all levels of excess II up to 1.0 wt.%. However, no
correlation was found between the amt. of excess II on the crossover
frequency or magnitude of the storage modulus and d. The crit.
shear stress at the wall obtained from the drag redn. data still
seemed to be the best single parameter to characterize the d of
viscoelastic surfactant formulations.
ST drag redn surfactant viscoelasticity; cationic surfactant drag redn
IT Viscoelastic materials
(cationic surfactant formulations, drag redn. and rheol.
properties of)
IT Flow
(drag redn. in, by viscoelastic cationic surfactant formulations)
IT Surfactants
(cationic, aq. solns. contg. sodium salicylate and, drag redn.
activity of, viscoelasticity in relation to)
IT Quaternary ammonium compounds, properties
RL: USES (Uses)
(trimethyltallow alkyl, salicylates, aq. solns. contg. sodium
salicylate and, drag redn. activity of, viscoelasticity in
relation to)
IT 54-21-7, Sodium salicylate
RL: USES (Uses)
(aq. solns. contg. quaternary ammonium salicylates and, drag
redn. activity of, viscoelasticity in relation to)
IT 61482-44-8 88928-16-9 120681-98-3 120681-99-4
RL: USES (Uses)
(aq. solns. contg. sodium salicylate and, drag redn. activity of,
viscoelasticity in relation to)
L4 ANSWER 14 OF 61 CA COPYRIGHT 1996 ACS
AN 107:200409 CA
TI Water-soluble hydrophobe association polymers
AU Evani, S.; ***Rose, G. D.***
CS Cent. Res., Dow Chem. Co., Midland, MI, 48640, USA
SO Polym. Mater. Sci. Eng. (1987), 57, 477-81
CODEN: PMSEDG; ISSN: 0743-0515
DT Journal; General Review
LA English
CC 42-0 (Coatings, Inks, and Related Products)
Section cross-reference(s): 38, 51
AB A review with 29 refs. on the development of water-sol. hydrophobe
assocn. polymer thickeners for control of latex paint rheol. and for
enhanced oil recovery.
ST associative thickener polymer review; rheol control coating
thickener review; oil recovery polymer thickener review
IT Thickening agents
(associative water-sol., polymers, for coating rheol. control and
enhanced oil recovery)
IT Rheology
(control of, of coatings, water-sol. associative polymer
thickeners for)
IT Polymers, uses and miscellaneous
RL: USES (Uses)
(thickeners, associative water-sol., for rheol. control)
IT Petroleum recovery
(thickening agents for, water-sol. hydrophobe associative
polymers as)
IT Coating materials
(latex, water-sol. associative polymer thickeners for, for
rhenol. control)
L4 ANSWER 15 OF 61 CA COPYRIGHT 1996 ACS
AN 106:136997 CA
TI Immobilization of yeast cells in polyurethane ionomers
AU Lorenz, O.; Haulena, F.; ***Rose, G.***
CS Fachhochsch. Aachen, Aachen, D-5100, Fed. Rep. Ger.
SO Biotechnol. Bioeng. (1987), 29(3), 388-91
CODEN: BIBIAU; ISSN: 0006-3592
DT Journal
LA English
CC 16-9 (Fermentation and Bioindustrial Chemistry)
AB Emulsifier-free aq. dispersions of amphiphilic polyurethane ionomers
were used for the immobilization of yeast cells. By coagulation
with a salt soln., mixts. of yeast cells and dispersion form
hydrogels under entrapment of the biocatalyst. Water channels form
the continuous phase of the hydrogels. As compared with other
polymers used for immobilization of cells or enzymes, polyurethane
ionomers offer certain advantages. (a) Immobilization is carried
out after formation of the polymer, which is free of unreacted NCO
groups; therefore, the polymer is nontoxic. (b) Caused by the
comparatively low swelling in water, the beads show a high mech.
stability. A further consequence of the low water swelling is the
possibility of forming gels with a high cell concn. (c) The
hydrophilicity of the ionomer can be varied within a broad range by
the type and amt. of the ionic groups, the nature of the counterion,
as well as the chem. structure of the macrodiol.
ST yeast immobilization polyurethane ionomer; Saccharomyces immobilized
urethane polymer
IT Fermentation
(ethanol, by yeast immobilized in polyurethane ionomers)
IT Saccharomyces cerevisiae
(immobilization of, in polyurethane ionomers)
IT Immobilization, biochemical
(of yeast, in polyurethane ionomers)
IT Urethane polymers, biological studies
RL: BIOL (Biological study)
(ionomers, yeast immobilization in)
IT 64-17-5P, Ethanol, preparation
RL: BMF (Bioindustrial manufacture); BIOL (Biological study); PREP
(Preparation)
(manuf. of, by yeast immobilized in polyurethane ionomers)
L4 ANSWER 16 OF 61 CA COPYRIGHT 1996 ACS
AN 106:121613 CA
TI The colloidal behavior of Kraft lignin and lignosulfonates
AU Nyman, Veronika; ***Rose, G.*** ; Ralston, J.
CS Dep. Appl. Chem., Swinburne Inst. Technol., Hawthorn, 3122,
Australia
SO Colloids Surf. (1986), 21, 125-47
CODEN: COSUD3; ISSN: 0166-6622
DT Journal
LA English
CC 43-5 (Cellulose, Lignin, Paper, and Other Wood Products)
AB Pinus radiata Kraft lignin [8068-05-1] (PKL), Eucalyptus regnans
kraft lignin (EKL) and Eucalyptus regnans NSSC lignosulfonic acid
[8062-15-5] (LSA) were isolated and purified. The PKL and LSA
samples were fractionated by gel permeation chromatog. and their
mol. wts. verified by light scattering. Mol. wts. ranged from 104
to 2.5 .times. 105. Coagulation studies of these lignins, as well
as 2 com. products (Indulin AT and Ufoxane 3A [8061-51-6]),
performed in the presence of salt indicated that the lignins behave
as colloids which are sterically stabilized, particularly at high
pH. Lignin specifically adsorbed onto solid Ca(OH)2 at pH 12.2 and
reversed the sign of the zeta potential. PKL, EKL, Indulin AT and
LSA were potentiometrically titrated. The variation of apparent
dissocn. const. with degree of dissocn. was markedly different from
that of classic polyelectrolytes. Aggregation effects occurred at
low .alpha., and surface chain extension and ionization at high
.alpha.. Most of the lignins had an intrinsic dissocn. const. (pK0)
equiv. to that of a carboxyl group. Free energy data and pK0 varied
with ionic strength in a manner which reflects the different chem.
structures of the 2 main classes of lignin.
ST kraft lignin colloidal property; lignosulfonic acid colloidal
property; dissocn kraft lignin lignosulfonic acid; zeta potential
kraft lignin lignosulfonic acid
IT Electrokinetic potential
(of kraft lignin from pine and eucalyptus and lignosulfonic acid,
colloidal properties in relation to)
IT 8061-51-6
RL: PRP (Properties)
(colloidal properties of, as model for kraft lignin from pine and
eucalyptus wood)
IT 8062-15-5, Lignosulfonic acid
RL: PRP (Properties)
(colloidal properties of, from eucalyptus)
IT 8068-05-1, Kraft lignin
RL: PRP (Properties)
(colloidal properties of, from pine and eucalyptus)
L4 ANSWER 17 OF 61 CA COPYRIGHT 1996 ACS
AN 105:112707 CA
TI Human polymorphic APO-LDL investigated by high-resolution
two-dimensional electrophoresis
AU De Benedictis, G.; Di Maio, E.; ***Rose, G.*** ; Renis, M.;
Brancati, C.; Tagarelli, A.
CS Dep. Cell Biol., Univ. Calabria, Arcavacata, 87030, Italy
SO Exp. Clin. Immunogenet. (1986), 3(2), 75-80
CODEN: ECIME4
DT Journal
LA English
CC 13-4 (Mammalian Biochemistry)
AB The apolipoprotein (APO) part of a human polymorphic
low-d.-lipoprotein (LDL) was investigated by 2-dimensional
electrophoresis. Since these allotypic LDLs were purified from sera
by specific immunochromatog., data are given for only 1 mol. species
of LDL. The 2-dimensional electrophoresis revealed the presence of
isoforms which were correlated to the serol. phenotype. A
hypothesis about APO-LDL gene organization is outlined.
ST apolipoprotein polymorphism phenotype
IT Genetics
(of apolipoproteins, of blood serum of humans)
IT Lipoproteins
RL: PRP (Properties)
(low-d. apo-, polymorphism of, of blood serum of humans)
L4 ANSWER 18 OF 61 CA COPYRIGHT 1996 ACS
AN 103:172024 CA
TI Dopaminergic neurotoxicity of 1-methyl-4-phenyl-1,2,3,6-
tetrahydropyridine (MPTP) in the mouse: an in vivo electrochemical
study
AU Gerhardt, G.; ***Rose, G.*** ; Stroemberg, I.; Conboy, G.; Olson,
L.; Jonsson, G.; Hoffer, B.
CS Health Sci. Cent., Univ. Colorado, Denver, CO, USA
SO J. Pharmacol. Exp. Ther. (1985), 235(1), 259-65
CODEN: JPETAB; ISSN: 0022-3565
DT Journal
LA English
CC 1-11 (Pharmacology)
AB The long-term (i.e., 4-5 mo) effects of large doses (3 .times. 50
mg/kg) of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)
[28289-54-5] on striatal dopamine [51-61-6]-contg. afferents were
studied in mice. There was a decrease in the av. K+-evoked release
of electroactive species from the MPTP-treated mouse caudate nucleus
vs. control. Greater decreases in release were seen in dorsal than
in ventral striatum. The av. rise time of K+-evoked release was
also prolonged after MPTP pretreatment. Histochem. studies showed
an overall redn. in the d. of dopamine-contg. terminals in the
drug-treated mice, with a greater loss obsd. in the more dorsal
regions of the caudate nucleus. The exptl. data thus support a
long-term selective destruction of dorsal vs. ventral
dopamine-contg. afferents to the striatum by the neurotoxin MPTP in
mice.
ST methylphenyltetrahydropyridine dopaminergic neuron toxicity brain
IT Nervous system
(central, dopaminergic, methylphenyltetrahydropyridine toxicity
to)
IT Brain, toxic chemical and physical damage
(striatum, methylphenyltetrahydropyridine toxicity to,
dopaminergic neuron in)
IT 51-61-6, biological studies
RL: BIOL (Biological study)
(brain striatum neurons contg., methylphenyltetrahydropyridine-
induced toxicity to)
IT 28289-54-5
RL: PRP (Properties)
(toxicity of, to dopaminergic neurons of brain striatum)
L4 ANSWER 19 OF 61 CA COPYRIGHT 1996 ACS
AN 103:116908 CA
TI Monoamine release from dopamine-depleted rat caudate nucleus
reinnervated by substantia nigra transplants: an in vivo
electrochemical study
AU ***Rose, G.*** ; Gerhardt, G.; Stroemberg, I.; Olson, L.; Hoffer,
B.
CS Health Sci. Cent., Univ. Colorado, Denver, CO, 80262, USA
SO Brain Res. (1985), 341(1), 92-100
CODEN: BRREAP; ISSN: 0006-8993
DT Journal
LA English
CC 2-8 (Mammalian Hormones)
AB In vivo electrochem. was used to analyze the magnitude, time course,
and spatial distribution of neurotransmitter releases evoked by
local application of K+ from dopamine (DA) [51-61-6]-depleted,
fetal substantial nigra (SN) transplant-reinnervated striatum.
Animals were injected unilaterally with 6-hydroxydopamine (6-OHDA)
into the SN and screened by measuring apomorphine [58-00-4]-induced
rotation. Some were then given SN grafts, which were placed in a
delayed cavity just dorsal to the lesioned striatum. Nafion-coated
graphite epoxy capillary (GEC) electrodes were employed for the
electrochem. to minimize signals derived from ascorbate or acidic DA
metabolites. The GEC electrode was fixed to a K+-filled
micropipette and this assembly was used to map the caudate nucleus
of control, 6-OHDA-treated, and 6-OHDA-treated, grafted animals.
The morphometric relations between striatal recording sites and
transplant location were subsequently verified histol. Release from
striatals sites within 1.0 mm of the SN grafts were slightly, but
not significantly, less than those obtained from control caudate.
By contrast, releases from striatal sites further distal from
transplants were markedly reduced to .apprx.30% of control; similar
values were obtained from 6-OHDA-treated striata which did not
received SN grafts. The time course of the K+-evoked releases was
also reduced following -OHDA treatment, but returned to control
values in striatal sites proximal to a transplant. Apparently SN
grafts ameliorate lesion-induced behavioral dysfunctions by
providing specific DA input to the host brain.
ST monoamine brain dopamine depletion transplant; behavior brain
dopamine depletion transplant
IT Transplant and Transplantation, animal
(of brain substantia nigra, momoamine release by striatum
response to, after dopamine depletion)
IT Nerve
(dopaminergic, brain striatum innervation by, from substantia
nigra transplant)
IT Embryo
(fetus, monoamine release by dopamine-depleted striatum response
to substantia nigra transplant from)
IT Amines, biological studies
RL: BIOL (Biological study)
(mono-, release of, by brain striatum after dopamine depletion,
substantia nigra transplant effect on)
IT Brain, metabolism
(striatum, monoamine release by, after dopamine depletion,
substantia nigra transplant effect on)
IT Brain
(substantia nigra, monoamine release by dopamine-depleted
striatum response to transplant of)
IT 51-61-6, biological studies
RL: BIOL (Biological study)
(depletion of, in brain striatum, monoamine release response to,
substantia nigra transplant effect on)
IT 7440-09-7, biological studies
RL: BIOL (Biological study)
(monoamine release stimulation by, in brain striatum after
dopamine depletion, substantia nigra transplant effect on)
IT 58-00-4
RL: BIOL (Biological study)
(rotational behavior response to, in dopamine depletion of
striatum, substantia nigra transplant effect on)
L4 ANSWER 20 OF 61 CA COPYRIGHT 1996 ACS
AN 102:129441 CA
TI Sequential changes in red cell glycolytic enzymes and intermediates
and possible control mechanisms in the first two months of postnatal
life in lambs
AU Travis, S. F.; Wagerle, L. C.; De Alvarado, C. M.; ***Rose, G.***
; Delivoria-Papadopoulos, M.
CS Jefferson Med. Coll., Thomas Jefferson Univ., Philadelphia, PA,
19107, USA
SO Pediatr. Res. (1985), 19(3), 272-7
CODEN: PEREBL; ISSN: 0031-3998
DT Journal
LA English
CC 13-3 (Mammalian Biochemistry)
AB The sequential changes in several red blood cell glycolytic enzymes,
glucose 6-phosphate dehydrogenase, glycolytic intermediates, and
ATP, as well as intracellular pH and plasma inorg. P, were followed
simultaneously in lambs from birth to 2 mo of age. The activities
of all glycolytic enzymes and glucose 6-phosphate dehydrogenase were
elevated at birth. The 2,3-DPG concn. increased markedly
postnatally and was assocd. with a simultaneous increase in the
concns. of red cell glucose 6-phosphate and total triose phosphate
and a decrease in intracellular pH. Inorg. P also increased and
correlated with the 2,3-DPG concn. in the 1st 10 days of postnatal
life. The content of red cell 3-phosphoglycerate,
2-phosphoglycerate, phosphoenolpyruvate, and ATP increased slightly.
These results suggested increased glycolytic flux through the
diphosphoglycerate mutase reaction which resulted in net synthesis
of 2,3-DPG. The red cell total triose phosphate peaked and fell
initially, followed by glucose 6-phosphate and 2,3-DPG, suggesting
inhibition of phosphofructokinase activity and a decrease in
glycolysis secondary to decreased red cell intracellular pH. After
10 days of postnatal life, all glycolytic intermediates fell
simultaneously, which correlated with a decrease in activity of the
glycolytic enzymes.
ST erythrocyte glycolysis newborn sheep; enzyme glycolysis newborn
sheep erythrocyte; development erythrocyte glycolysis sheep
IT Glycolysis
(by erythrocytes, of newborn sheep, regulatory mechanisms in
relation to)
IT Sheep
(glycolysis by erythrocytes of newborn of)
IT Development, mammalian
(glycolysis by erythrocytes of sheep in)
IT Newborn
(glycolysis by erythrocytes of, of sheep)
IT Erythrocyte
(glycolytic enzymes and intermediates of, of newborn sheep,
regulatory mechanisms in relation to)
IT Acid-base equilibrium
(of erythrocytes, of newborn sheep)
IT Blood plasma
(phosphorus of, of newborn sheep)
IT Enzymes
RL: BIOL (Biological study)
(glycolytic, of erythrocytes of newborn sheep)
IT Carbohydrates and Sugars, esters
RL: BIOL (Biological study)
(trioses, phosphates, of erythrocytes of newborn sheep)
IT 7723-14-0, biological studies
RL: BIOL (Biological study)
(of blood plasma, of newborn sheep)
IT 56-73-5 138-08-9 138-81-8 643-13-0 820-11-1 9001-40-5
9001-51-8 9001-59-6 9001-80-3 9001-83-6 9014-08-8
9023-91-0 9024-52-6 25535-59-5
RL: BIOL (Biological study)
(of erythrocytes, of newborn sheep)
L4 ANSWER 21 OF 61 CA COPYRIGHT 1996 ACS
AN 102:83585 CA
TI Centralized mining environment monitoring system CGA
AU Boutonnat, M.; Marget, C.; ***Rose, G.***
CS Fr.
SO Ind. Miner., Tech. (1984), (7), 592-8
CODEN: INMTDT; ISSN: 0240-9542
DT Journal
LA French
CC 59-1 (Air Pollution and Industrial Hygiene)
Section cross-reference(s): 51, 79
AB A centralized system for monitoring air quality in mines (e.g.,
firedamp levels in ventilation and degassing pipes, air speed, CO
and CO2 levels, temp.) is based on an above-ground microcomputer
connected to surface modems, subsurface modems, and subsurface
samplers through telemetric long lines. All air quality data is
centralized and visualized on the surface using printers, graphical
printers, etc. The monitoring system is designed to run
independently of mining operations. The structure of the system is
modular and adaptable. Good results were obtained from exptl. use
of the system at a coal mining office in Lorraine in Oct., 1982.
ST mining air quality monitoring microcomputer; coal mine environment
monitoring microcomputer
IT Computer application
(in centralized air quality monitoring system in mines)
IT Air analysis
(in mines, centralized computerized system for)
IT Firedamp
(monitoring of, in coal mines, centralized computer system for)
IT Mines and Mining
(coal, air quality monitoring in, centralized computer system
for)
IT 74-82-8, analysis 630-08-0, analysis
RL: ANST (Analytical study)
(monitoring of, in coal mine air, centralized system for)
L4 ANSWER 22 OF 61 CA COPYRIGHT 1996 ACS
AN 101:94149 CA
TI Fundamental studies on coal gasification mechanisms
AU Zabransky, R. F.; Stock, L. M.; ***Rose, G.***
CS Inst. Gas Technol., Chicago, IL, USA
SO Report (1983), GRI-81/0198; Order No. PB84-148063, 41 pp. Avail.:
NTIS
From: Gov. Rep. Announce. Index (U. S.) 1984, 84(7), 204
DT Report
LA English
CC 51-20 (Fossil Fuels, Derivatives, and Related Products)
AB Data on the pyrolytic reactivity of structural elements in coal were
obtained by converting Illinois No. 6 coal into O- and C-alkylated
coals, some contg. 13C and D labels including the O-Me, O-benzyl,
O-benzyl-d7, O-benzyl-1-13C, C-benzyl-d7, and C-benzyl-1-13C derivs.
The modified coals are more reactive than the unmodified, which
suggests that the extent of small-fragment-mol. formation depends in
a direct way upon the concn. of radicals within the coal particles.
The exchange patterns suggest that the energetically more favorable
reactions occur reversibly, and that the radical-addn. and
recombination reactions compete favorably with fragmentation and
radical-substitution reactions. The nonrandom distribution of the
isotopic labels in the products indicates that the reactions within
the coal particles are kinetically controlled, even at >850.degree..
ST coal gasification mechanism alkylation; radical coal gasification
alkylation; kinetics coal gasification isotope; pyrolysis coal
gasification
IT Radicals, reactions
RL: RCT (Reactant)
(in pyrolytic coal gasification)
IT Thermal decomposition
(mechanism of, in coal gasification)
IT Benzylation
Methylation
(of coal, coal-gasification mechanism in relation to)
IT Coal gasification
(pyrolysis, radical reactions in)
L4 ANSWER 23 OF 61 CA COPYRIGHT 1996 ACS
AN 101:91525 CA
TI Isocyanato prepolymers of diisocyanates containing differently
reactive NCO-groups
AU Lorenz, O.; Decker, H.; ***Rose, G.***
CS Fachhochsch. Aachen, Aachen, D-5100, Fed. Rep. Ger.
SO Angew. Makromol. Chem. (1984), 122, 83-99
CODEN: ANMCBO; ISSN: 0003-3146
DT Journal
LA German
CC 35-3 (Chemistry of Synthetic High Polymers)
Section cross-reference(s): 22, 67
AB Two methods are described for detg. the ratio (.gamma.) of the rate
consts. for urethane formation by isocyanates having 2 NCO groups of
differing reactivity. In the reaction of hexamethylene diisocyanate
[822-06-0] or isophorone diisocyanate [4098-71-9] with excess BuOH
[71-36-3], the consumption of both NCO groups follows 1st-order
kinetics. The .gamma. so detd. is 1.0 and 5.1-4.4, resp., at
40-65.degree.. In the reaction of excess diisocyanate with
macrodiols, e.g. polytetramethylene glycol [25190-06-1], .gamma.
can be estd. from NCO consumption provided that when .gamma. is not
1, the reaction is 1st-order for both NCO groups. Under these
conditions, and knowing .gamma., product compn., diisocyanates
singly or doubly bonded, and the type of NCO end groups on
prepolymers can be calcd.
ST isocyanate reactivity ratio diisocyanate; hexamethylene diisocyanate
reactivity ratio; isophorone diisocyanate reactivity ratio; butanol
reaction diisocyanate kinetics; polytetramethylene glycol reaction
diisocyanate; kinetics reaction alc diisocyanate; polyurethane compn
diisocyanate reactivity
IT Urethane polymers, properties
RL: PRP (Properties)
(compn. of, diisocyanate reactivity ratio in relation to)
IT Kinetics of polymerization
(of diisocyanates with polymeric diols, isocyanate group
reactivity ratio in relation to)
IT Kinetics of esterification
(of diisocyanates, isocyanate group reactivity ratio in relation
to)
IT 822-06-0 4098-71-9
RL: RCT (Reactant)
(reaction of, with alcs., isocyanate group reactivity ratio in)
IT 71-36-3, reactions 25190-06-1
RL: RCT (Reactant)
(reaction of, with diisocyanates, isocyanate group reactivity
ratio in)
L4 ANSWER 24 OF 61 CA COPYRIGHT 1996 ACS
AN 100:104292 CA
TI Separation of PUR-ionomers with sulfonate groups and nonionic
prepolymers using gel-permeation chromatography
AU Lorenz, O.; ***Rose, G.***
CS Fachbereich 3, Fachhochsch. Aachen, Aachen, Fed. Rep. Ger.
SO Angew. Makromol. Chem. (1983), 118, 91-104
CODEN: ANMCBO; ISSN: 0003-3146
DT Journal
LA German
CC 37-3 (Plastics Manufacture and Processing)
AB Ionomers were prepd. by the reaction of prepolymers (prepd. from
polypropylene glycol or polytetramethylene glycol and hexamethylene
or isophorone diisocyanates and purified by thin-film distn.) with
H2NCH2CH2NHCH2CH2SO3Na in varying amts. Sepn. of the products by
gel permeation chromatog. using .mu.-Bondagel packing and aq.
eluants gave ionomer-prepolymer compns. identical with those calcd.
for most probable mol. wt. distributions.
ST polyurethane ionomer gel chromatog; sulfoethylethylenediamine
polyurethane; ethylenediamine sulfoethyl polyurethane; polyether
polyurethane ionomeric
IT Urethane polymers, properties
RL: USES (Uses)
(ionomers, sepn. from nonionic, by gel chromatog.)
IT Ionomers
RL: USES (Uses)
(polyurethanes, sepn. from nonionic, by gel chromatog.)
IT 9048-90-2D, reaction products with [(aminoethyl)amino]ethanesulfonat
e 9082-83-1D, reaction products with [(aminoethyl)amino]ethanesulf
onate 34730-59-1D, reaction products with polyurethanes
39378-01-3D, reaction products with [(aminoethyl)amino]ethanesulfona
te
RL: PROC (Process)
(gel chromatog. of)
L4 ANSWER 25 OF 61 CA COPYRIGHT 1996 ACS
AN 98:90339 CA
TI Polyurethane ionomers from isocyanate prepolymers purified by
thin-film distillation
AU Lorenz, O.; ***Rose, G.***
CS Lab. Makromol. Chem., Fachhochsch., Aachen, D-5100, Fed. Rep. Ger.
SO Colloid Polym. Sci. (1982), 260(12), 1079-82
CODEN: CPMSB6; ISSN: 0303-402X
DT Journal
LA German
CC 37-3 (Plastics Manufacture and Processing)
AB NCO-contg. prepolymers were prepd. from 2021 g polytetramethylene
glycol (Teracol 2000) and 289.6 g hexamethylene diisocyanate (I) at
110.degree. and subjected to thin-film distn. to reduce the content
of free I from 2.4 to 1.1%. The prepolymers were chain extended
with H2NCH2CH2NHCH2CH2SO3Na and converted to anionic polyurethane
[80164-54-1] dispersions from acetone soln. The polydispersity and
av. particle size of the dispersion were decreased by decreasing the
amt. of free I.
ST polyurethane anionic latex; sulfonate aminoethyl polyurethane;
ethylenediamine sulfonate deriv polyurethane; distn thin film
polyurethane; particle size polyurethane latex; polydispersity
polyurethane latex
IT Urethane polymers, preparation
RL: SPN (Synthetic preparation); PREP (Preparation)
(latexes, prepolymer purifn. in prepn. of, particle size and
polydispersity in relation to)
IT Particle size
(of polyurethane latexes, prepolymer purifn. effect on)
IT 80164-54-1
RL: USES (Uses)
(latexes, particle size and polydispersity of, prepolymer purifn.
effect on)
L4 ANSWER 26 OF 61 CA COPYRIGHT 1996 ACS
AN 96:200611 CA
TI Determination of strong acid near weak acid in polyurethane
dispersions with sulfonate and carboxylate groups
AU Lorenz, O.; Breidenich, N.; Denter, U.; Reinmoeller, K. H.;
***Rose, G.***
CS Lab. Makromol. Chem., Fachhochsch. Aachen, Aachen, Fed. Rep. Ger.
SO Angew. Makromol. Chem. (1982), 103, 159-85
CODEN: ANMCBO; ISSN: 0003-3146
DT Journal
LA German
CC 37-1 (Plastics Manufacture and Processing)
AB Dispersions of polyurethanes contg. varying amts. of SO3- and/or
CO2- groups are prepd. by the reaction of polytetramethylene ether
glycol (I) or a I-trimellitic anhydride copolymer with OCN(CH2)6NCO
followed by chain extension with 2,2-dimethylolpropionic acid
triethylamine salt and/or H(NHCH2CH2)2SO3Na. The dispersions are
analyzed for strong and weak acid groups after cation exchange
against H+ or Ag+ by conductometric and potentiometric titrns.
While the conductometric titrn. of Ag+ ions with NaCl represents a
very reliable method for the detn. of the sum of strong and weak
acid, the endpoints during neutralization with NaOH are often
incorrect or difficult to evaluate. However, the conductometric
neutralization in the presence of a salt (KBr) distinguishes quant.
between strong and weak acid, as the acid strength of the SO3-
groups increases by addn. of the salt. The replacement of CO2-
groups in a salt by conductometric titrn. with a strong acid, such
as HCl, represents a method for detg. the weak acid.
Polyelectrolytes formed as by-products can be analyzed in the serum
by these methods after coagulation of the dispersed particles by
freezing. The sepn. of polyelectrolytes with CO2- groups by anion
exchange does not proceed quant. contrary to those with SO3- groups.
ST polyurethane ionomer detn dispersion; carboxy group detn
polyurethane; sulfo group detn polyurethane; conductometry detn
polyurethane ionomer; potentiometry detn polyurethane ionomer
IT Urethane polymers, analysis
RL: PRP (Properties)
(detn. of strong and weak acid groups in, by conductometric and
potentiometric titrn.)
IT Titration
(conductometric, of polyurethanes contg. strong and weak acid
groups)
IT Ionomers
RL: PRP (Properties)
(polyurethanes, detn. of strong and weak acid groups in, by
conductometric and potentiometric titrn.)
IT Titration
(potentiometric, of polyurethanes contg. strong and weak acid
groups)
IT 80164-54-1 81766-89-4
RL: PRP (Properties)
(detn. of acid groups in, by conductometric and potentiometric
titrn.)
IT 81766-91-8 81830-17-3
RL: PRP (Properties)
(detn. of strong and weak acid groups in, by conductometric and
potentiometric titrn.)
L4 ANSWER 27 OF 61 CA COPYRIGHT 1996 ACS
AN 95:151587 CA
TI Effect of water-soluble polyelectrolytes from 1,6-hexamethylene
diisocyanate and sodium N-(2-aminoethyl)-2-aminoethanesulfonate on
the dispersion formation by anionic polyurethanes
AU Lorenz, O.; ***Rose, G.***
CS Lab. Makromol. Chem., Fachhochsch. Aachen, Aachen, 5100, Fed. Rep.
Ger.
SO Colloid Polym. Sci. (1981), 259(6), 587-95
CODEN: CPMSB6; ISSN: 0303-402X
DT Journal
LA German
CC 36-6 (Plastics Manufacture and Processing)
AB Solns. of polyelectrolytes prepd. by treating 1 or 2 mol
1,6-hexamethylene diisocyanate (I) with 1 mol Na
N-(2-aminoethyl)-2-aminoethanesulfonate (II) were added to acetone
solns. of an anionic polyurethane [65328-15-6] (prepd. from I, II,
and an adipic acid-2,2-dimethyl-1,3-propanediol-1,6-hexanediol
copolymer) before formation of an aq. dispersion. Continuous cond.
measurements during dispersion showed that above a certain water
concn. the cond. decreased with increasing amt. of polyelectrolyte.
This was attributed to a partially reversible assocn. of particles
with inclusion of water between the assocd. particles. The mean
particle diam. increased with increasing polyelectrolyte content.
The assocn. of particles became largely irreversible above a crit.
concn. of polyelectrolyte, preventing the formation of stable
dispersions.
ST polyelectrolyte dispersion formation polyurethane; hexamethylene
diisocyanate copolymer polyelectrolyte; aminoethanesulfonate
copolymer polyelectrolyte
IT Urethane polymers, properties
RL: PRP (Properties)
(anionic, dispersion formation by, polyelectrolyte effect on)
IT Dispersion
(of anionic urethane polymers in water, polyelectrolyte effect
on)
IT 65328-15-6
RL: USES (Uses)
(dispersion formation by, polyelectrolyte effect on)
IT 63532-93-4
RL: USES (Uses)
(dispersion formation of anionic polyurethanes in presence of)
L4 ANSWER 28 OF 61 CA COPYRIGHT 1996 ACS
AN 95:148679 CA
TI Degradation of steroids by microorganisms. XVII. 11.beta.- and
12.beta.-hydroxylation of (20S)-20-carboxy-1,4-pregnadien-3-one by
Cochliobolus lunatus
AU Hoerhold, C.; ***Rose, G.*** ; Kaufmann, G.
CS Forschungszent. Molekularbiol. Med., DAW, Jena, DDR-69, Ger. Dem.
Rep.
SO Z. Allg. Mikrobiol. (1981), 21(4), 289-93
CODEN: ZAPOAK; ISSN: 0044-2208
DT Journal
LA German
CC 16-5 (Fermentations)
Section cross-reference(s): 32
AB 11.beta.- [75220-09-6] And 12.beta.-hydroxy-(20S)-20-carboxy-1,4-
pregnadien-3-one [78962-23-9] were produced in 20 and 13% yield,
resp., from (20S)-20-carboxy-1,4-pregnadien-3-one [71154-85-3] by
C. lunatus. The use of microbial metabolites of the
20-carboxypregnane type for the partial synthesis of
glucocorticosteroid is discussed.
ST steroid hydroxylation Cochliobolus
IT Hydroxylation
(11.beta.- and 12.beta.-, of carboxypregnadienone by Cochliobolus
lunatus)
IT Cochliobolus lunatus
(carboxypregnadienone hydroxylation by)
IT 71154-85-3
RL: RCT (Reactant)
(hydroxylation of, by Cochliobolus lunatus)
IT 75220-09-6P 78962-23-9P
RL: PREP (Preparation)
(prepn. of, with Cochliobolus lunatus)
L4 ANSWER 29 OF 61 CA COPYRIGHT 1996 ACS
AN 95:4163 CA
TI Selective uptake and anterograde transport of horseradish peroxidase
by hippocampal granule cells
AU Erzurumlu, R. S.; ***Rose, G.*** ; Lynch, G. S.; Killackey, H. P.
CS Sch. Social Sci., Univ. California, Irvine, CA, 92717, USA
SO Neuroscience (1981), 6(5), 897-902
CODEN: NRSCDN; ISSN: 0306-4522
DT Journal
LA English
CC 13-2 (Mammalian Biochemistry)
AB Introduction of horseradish peroxidase into the ventriculocisternal
system results in selective labeling of the granule cells of the
dentate gyrus and their axons, the mossy fibers. This labeling
pattern is not seen after direct injections of horseradish
peroxidase into the dorsal hippocampus. The d. of the granule cell
labeling appears to be related to their proximity to the site of
highest horseradish peroxidase concn. The combined distribution of
horseradish peroxidase in the granule cells and mossy fibers
strongly suggests that the latter element is labeled as the result
of anterograde transport of horseradish peroxidase taken up by the
granule cell perikarya or dendrites. This labeling was found in the
absence of injury to the hippocampus, suggesting that neuronal
damage is not necessary for anterograde transport horseradish
peroxidase to occur.
ST peroxidase axonal transport hippocampus; brain peroxidase axonal
transport
IT Brain, metabolism
(axon, peroxidase axonal transport by, of hippocampus)
IT Brain, metabolism
(hippocampus, peroxidase axonal transport by)
IT 9003-99-0
RL: PROC (Process)
(axonal transport of, by hippocampus)
L4 ANSWER 30 OF 61 CA COPYRIGHT 1996 ACS
AN 94:186891 CA
TI Modular assembly of proteins
AU Wetlaufer, D. B.; ***Rose, G. D.***
CS Dep. Chem., Univ. Delaware, Newark, DE, USA
SO Biomol. Struct., Conform., Funct., Evol., Proc. Int. Symp. (1981),
Meeting Date 1978, Volume 2, 97-101. Editor(s): Srinivasan,
Ramachandran; Subramanian, E.; Yathindra, N. Publisher: Pergamon,
Oxford, Engl.
CODEN: 45JXAX
DT Conference; General Review
LA English
CC 6-0 (General Biochemistry)
AB A review and discussion with 18 refs.
ST review protein modular assembly
IT Chains, chemical
(folding of, of proteins)
IT Proteins
RL: BIOL (Biological study)
(modular assembly of)
L4 ANSWER 31 OF 61 CA COPYRIGHT 1996 ACS
AN 92:133620 CA
TI Corrosion behavior of cast nickel aluminum bronze in sea water
AU Culpan, E. A.; ***Rose, G.***
CS Admir. Underwater Weapons Establ., Portland/Dorset, Engl.
SO Br. Corros. J. (1979), 14(3), 160-6
CODEN: BCRJA3; ISSN: 0007-0599
DT Journal
LA English
CC 56-8 (Nonferrous Metals and Alloys)
AB Sea water corrosion of cast, heat-treated, and welded bronze
[73134-99-3] contg. Al 9.5, Ni 4.7, Fe 4.3, and Mn 1% was followed
by optical and electron microscopy. Selective phase corrosion
occurred near the weld heat-affected zone due to attack of the
.alpha.-phase adjacent the continuous lamellar .kappa.-phase. Heat
treatment considerably decreased the corrosion susceptibility due to
stress relief, dispersal of the .kappa.-phase, and pptn. of finely
dispersed cathodic phases within the .alpha.-matrix.
ST bronze microstructure corrosion seawater; weld bronze seawater
corrosion
IT Welds
(bronze, corrosion of, in seawater)
IT 73134-99-3
RL: USES (Uses)
(corrosion of cast, in seawater, microstructure effect on)
L4 ANSWER 32 OF 61 CA COPYRIGHT 1996 ACS
AN 92:132435 CA
TI Results of conductivity, ion mobility and ion concentration
measurements obtained with a parachuted Gerdien aspiration analyzer
probe in heights below 70 km
AU Widdel, H. U.; ***Rose, G.*** ; Borchers, R.
CS Max-Planck-Inst. Aeron., Katlenburg-Lindau, D-3411/3, Fed. Rep. Ger.
SO J. Atmos. Terr. Phys. (1979), 41(10-11), 1141-7
CODEN: JATPA3; ISSN: 0021-9169
DT Journal
LA English
CC 53-10 (Mineralogical and Geological Chemistry)
AB The results of cond., ion mobility, and ion cond. measurements
performed below 70 km with a parachuted Gerdien aspiration analyzer
during winter and in the summer season are described. The mobility
of the most abundant species of pos. ions was the same for summer
and winter conditions. Obsd. increases of cond. are caused by
increased carrier d. Increases of neg. cond. in heights above 40 km
found in the winter seasons were probably caused by an increase of
the no. d. of free electrons. A direct linear relation between the
no. d. of charged carriers and the air temp. was not found.
Suggestions are made for the cause of the obsd. seasonal variation
in ion d. and in .lambda., the ratio of neg. ions to electrons.
ST atm ion cond concn detn
IT Atmosphere
(cond. and ion mobility and ion concn. measurements in)
L4 ANSWER 33 OF 61 CA COPYRIGHT 1996 ACS
AN 92:104947 CA
TI Steroid converting enzyme from microorganisms. XIII. Relation
between steroid structure and induction of 4-ene-3-
oxosteroid:(acceptor)-1-ene-oxidoreductase in Nocradia opaca
AU Hoerhold, C.; Hueller, E.; ***Rose, G.***
CS Zentralinst. Mikrobiol. Exp. Ther., DAW, Jena, Ger. Dem. Rep.
SO Z. Allg. Mikrobiol. (1980), 20(1), 23-32
CODEN: ZAPOAK; ISSN: 0044-2208
DT Journal
LA German
CC 3-2 (Biochemical Interactions)
AB Induction of the title enzyme in N. opaca by steroids was dependent
on both hydrophobic and hydrophilic characteristics of the inducer
mol., being influenced, for example, by the presence of oxygen
functions and Me groups on the inducer. Another factor that must be
considered results from the degrdn. of the steroid during the period
of enzyme induction.
ST steroid dehydrogenase induction; Nocardia steroid dehydrogenase
induction
IT Nocardia opaca
(steroid dehydrogenase formation by, steroid induction of)
IT Molecular structure-biological activity relationship
(steroid dehydrogenase-inducing, of steroids)
IT 9029-04-3
RL: FORM (Formation, nonpreparative)
(formation of, by Nocardia opaca, steroid induction of)
IT 50-23-7 50-24-8 50-28-2, biological studies 52-76-6 53-03-2
53-06-5 57-63-6 57-83-0, biological studies 58-18-4 58-22-0
63-05-8 64-85-7 68-96-2 72-63-9 152-58-9 302-22-7
434-22-0 566-35-8 1093-58-9 1164-81-4 2446-23-3 5785-58-0
19590-23-9 20592-45-4 24284-83-1 43085-16-1 56102-66-0
63795-53-9 63795-83-5 63795-84-6 65928-56-5
RL: PRP (Properties)
(steroid dehydrogenase induction by, in Nocardia opaca)
L4 ANSWER 34 OF 61 CA COPYRIGHT 1996 ACS
AN 92:36860 CA
TI Steroid converting enzymes from microorganisms. XII.
Characteristics of the induction of 4-en-3-oxosteroid:
(acceptor)-1-en-oxidoreductase in Nocardia opaca
AU Hoerhold, C.; Hueller, E.; ***Rose, G.***
CS Zentralinst. Mikrobiol. Exp. Ther., DAW, Jena, DDR 69, Ger. Dem.
Rep.
SO Z. Allg. Mikrobiol. (1979), 19(10), 731-9
CODEN: ZAPOAK; ISSN: 0044-2208
DT Journal
LA German
CC 7-13 (Enzymes)
Section cross-reference(s): 10
AB 17.alpha.-Methyltestosterone (I) and the corresponding 1(2)-dehydro
compd., Dianabol, were efficient inducers of the
4-en-3-oxosteroid-acceptor 1-en-oxidoreductase (EC 1.3.99.4) (II) of
N. opaca. After a 4 h lag period, II activity increased, reaching
an optimum value between 8 and 12 h and then decreasing to its
original value by 48 h. The steroids were completely metabolized
after 12 h, corresponding to the drop in II activity. The optimum I
concn. for induction was 0.3-0.4 mg/mL, higher concns. causing
reduced II activity. The optimum temp. for induction by 0.4 mg/mL I
was between 25 and 31.5.degree.; at 34.degree., the activity sharply
decreased and at 37.degree. it was undetectable. Chloramphenicol
and streptomycin were powerful inhibitors of the induction process,
causing 85% inhibition at a concn. of 8 .mu.M.
ST steroid dehydrogenase Nocardia induction methyltestosterone;
Dianabol induction steroid dehydrogenase Nocardia
IT Nocardia opaca
(oxosteroid .DELTA.1-dehydrogenase of, induction of, by
methyltestosterone and Dianabol)
IT 9029-04-3
RL: BIOL (Biological study)
(of Nocardia opaca, induction of, by methyltestosterone and
Dianabol)
IT 56-75-7 57-92-1, biological studies
RL: BIOL (Biological study)
(oxosteroid .DELTA.1-dehydrogenase of Nocardia induction by
steroid inhibition by)
IT 58-18-4 72-63-9
RL: BIOL (Biological study)
(oxosteroid .DELTA.1-dehydrogenase of Nocaridia opaca induction
by)
L4 ANSWER 35 OF 61 CA COPYRIGHT 1996 ACS
AN 92:20933 CA
TI Atherosclerosis as related to diet
AU Tunstall Pedoe, H.; ***Rose, G.***
CS St. Mary's Hosp. Med. Sch., London, Engl.
SO Int. Rev. Biochem. (1979), 27(Biochem. Nutr. 1), 245-79
CODEN: IRBID3; ISSN: 0147-7366
DT Journal; General Review
LA English
CC 18-0 (Animal Nutrition)
AB A review with 161 refs.
ST review atherosclerosis diet
IT Diet
(atherosclerosis in relation to)
IT Atherosclerosis
(diet in relation to)
L4 ANSWER 36 OF 61 CA COPYRIGHT 1996 ACS
AN 91:163954 CA
TI Thermodynamic parameters of liquid gold-aluminum alloys
AU Erdelyi, L.; Tomiska, J.; Neckel, A.; ***Rose, G.*** ;
Ramakrishnan, E. S.; Fabian, D. J.
CS Tech. Univ. Vienna, Vienna, Austria
SO Metall. Trans., A (1979), 10A(10), 1437-43
CODEN: MTTABN; ISSN: 0360-2133
DT Journal
LA English
CC 69-1 (Thermodynamics, Thermochemistry, and Thermal Properties)
Section cross-reference(s): 56, 68
AB Thermodn. activities and enthalpies for Au-Al alloys were measured
by Knudsen-cell mass spectrometry. The results are consistent and
indicate, for Au rich alloys, gold activities with pos. deviations
from Raoult ideality. This is in disagreement with emf.
measurements of Au activity previously reported; the results also
indicate endothermicities that are some 5-6 kJ/mol larger than those
indicated by the emf measurements.
ST heat alloying gold aluminum; gold aluminum alloying thermodn;
activity aluminum gold liq alloy
IT Free energy
Thermodynamics
(of alloying, of aluminum with gold, in liq. state)
IT Heat of alloying
(of aluminum with gold, in liq. state)
IT Activity
(of gold, in aluminum-gold liq. alloys)
IT 39285-21-7
RL: PRP (Properties)
(thermodn. of alloying of liqs.)
L4 ANSWER 37 OF 61 CA COPYRIGHT 1996 ACS
AN 91:161573 CA
TI Microstructural characterization of cast nickel aluminum bronze
AU Culpan, E. A.; ***Rose, G.***
CS Admiralty Underwater Weapons Establ., Portland, Engl.
SO Report (1978), AUWE-TN-580/78, AUWE-ACC-46194, DRIC-BR-65483; Order
No. AD-A063091, 33 pp. Avail.: NTIS
From: Gov. Rep. Announce. Index (U. S.) 1979, 79(10), 155
DT Report
LA English
CC 56-6 (Nonferrous Metals and Alloys)
AB The morphol. and chem. anal. of the complex phases present in cast
Ni Al bronze [39325-63-8] contg. Al 10, Ni 5, and Fe 5% were detd.
by metallog., SEM, and scanning transmission electron microscropy,
coupled to an energy dispersive anal. system. The development of
structure was detd. from liq. metal to the room temp., including the
modifications produced by heat treatment.
ST bronze structure phase analysis; aluminum nickel bronze structure
IT 39325-63-8
RL: USES (Uses)
(morphol. of cast, phase anal. for)
L4 ANSWER 38 OF 61 CA COPYRIGHT 1996 ACS
AN 90:214459 CA
TI Spectrometric studies on N,N'-disubstituted dithiomalonamides and
their cobalt(II) complexes
AU Schleinitz, K. D.; ***Rose, G.*** ; Kunzek, H.; Koeppel, H.
CS Sekt. Chem., Humboldt-Univ., Berlin, E. Ger.
SO J. Prakt. Chem. (1979), 321(1), 1-7
CODEN: JPCEAO; ISSN: 0021-8383
DT Journal
LA German
CC 78-7 (Inorganic Chemicals and Reactions)
Section cross-reference(s): 73
AB CoL2 (HL = RNHCSCH2CSNHR, where R = Me, Ph, m-ClC6H4, p-ClC6H4,
m-NO2C6H4) were prepd. by reaction of Co(OAc)2 with HL. The
complexes were characterized by UV-visible, IR, ESR, and NMR
spectra. These Co(II) complexes are S4-coordinated square planar
complexes. The orbital splitting parameters of CoL2 were calcd. and
are <20,000 cm-1. The spectrochem. series for CoL2 is (with respect
to R): Me < m-ClC6H4 < m-NO2C6H4 < p-ClC6H4 < Ph.
ST cobalt dithiomalonamide; energy level splitting cobalt
dithiomalonamide; thiomalonamide cobalt; malonamide dithio cobalt;
UV cobalt dithiomalonamide; IR cobalt dithiomalonamide; NMR cobalt
dithiomalonamide
IT Infrared spectra
Nuclear magnetic resonance
Ultraviolet and visible spectra
(of cobalt complexes with disubstituted dithiomalonamides)
IT Energy level splitting
(crystal-field, of cobalt complexes with disubstituted
dithiomalonamides)
IT 70365-87-6P 70365-88-7P 70365-89-8P 70365-90-1P 70365-91-2P
RL: PRP (Properties); SPN (Synthetic preparation); PREP
(Preparation)
(prepn. and spectra of)
L4 ANSWER 39 OF 61 CA COPYRIGHT 1996 ACS
AN 90:81264 CA
TI In vitro inhibition of .DELTA.4-3-ketosteroid-5.alpha.-reductase
from rat liver by steroids
AU Schubert, K.; Schumann, G.; ***Rose, G.*** ; Ritter, F.; Strecke,
J.; Schlegel, J.
CS Zentralinst. Mikrobiol. Exp. Ther., DAW, Jena, E. Ger.
SO Endokrinologie (1978), 72(2), 141-8
CODEN: ENDKAC; ISSN: 0013-7251
DT Journal
LA German
CC 2-3 (Hormone Pharmacology)
AB The inhibitory effects of pregnanes, androstanes, and estrogens on
the .DELTA.4-3-keto steroid 5.alpha.-reductase [9036-43-5] activity
in female rat liver microsomes was studied. In the pregnane series,
progesterone [57-83-0], 17.alpha.-hydroxyprogesterone [68-96-2],
and 17.alpha.-hydroxyprogesterone acetate [302-23-8] inhibited the
enzyme activity >90%. In the androstane and 19-norandrostane
series, the enzyme inhibitory effects of the androstane and
androstane acetates were similar. In the estratriene series,
ethynylestradiol [57-63-6] inhibited the enzyme activity
.apprx.90%. In this series, methylation of the phenolic hydroxyl
group decreased inhibitory activity. All 5 estriol derivs.
inhibited the enzyme .gtoreq.80%.
ST keto steroid reductase liver steroid; androstane testosterone
hydrogenation liver; pregnane testosterone hydrogenation liver;
estrogen testosterone hydrogenation liver; testosterone
hydrogenation liver steroid
IT Steroids, biological studies
RL: BIOL (Biological study)
(keto steroid reductase of liver microsome inhibition by)
IT Liver, composition
(keto steroid reductase of microsome of, steroids inhibition of)
IT Microsome
(keto steroid reductase of, of liver, steroids inhibition of)
IT Molecular structure-biological activity relationship
(keto steroid reductase-inhibiting, of steroids)
IT 58-22-0
RL: RCT (Reactant)
(hydrogenation of, by liver microsome, steroids effect on)
IT 50-27-1 50-27-1D, derivs. 50-28-2D, deriv. 57-63-6 57-83-0,
biological studies 57-83-0D, derivs. 64-85-7 68-22-4 68-23-5
68-96-2 80-75-1 302-22-7 302-23-8 302-76-1 434-03-7
434-22-0 516-15-4 604-19-3 974-76-5 1035-77-4 1096-38-4
1162-54-5 1162-56-7 1231-93-2 1424-00-6 4567-67-3
6533-00-2 15236-73-4 16669-06-0 18290-31-8 21887-09-2
24275-16-9 24284-83-1 24284-84-2 24749-37-9 24887-75-0D,
deriv. 34414-59-0 51946-28-2 51946-32-8 51946-43-1
51946-44-2 51946-45-3 54850-06-5 54982-79-5 63795-53-9
67192-96-5 67192-97-6 67473-36-3 68144-88-7 68144-94-5
68144-95-6 68169-59-5 69311-86-0 69311-87-1 69311-88-2
69311-89-3 69311-90-6
RL: BIOL (Biological study)
(keto steroid reductase of liver microsome inhibition by)
IT 128-23-4 566-65-4 600-57-7
RL: BIOL (Biological study)
(keto steroid reductase of liver microsomes in relation to)
IT 52-76-6 57-63-6 427-51-0 2098-66-0
RL: BIOL (Biological study)
(ketone steroid reductase of liver microsome in relation to)
IT 9036-43-5
RL: BIOL (Biological study)
(of liver microsome, steroids effect on)
L4 ANSWER 40 OF 61 CA COPYRIGHT 1996 ACS
AN 90:27489 CA
TI Microstructural characterization of cast nickel aluminum bronze
AU Culpan, E. A.; ***Rose, G.***
CS Admir. Underwater Weapons Establ., Portland/Dorset, Engl.
SO J. Mater. Sci. (1978), 13(8), 1647-57
CODEN: JMTSAS; ISSN: 0022-2461
DT Journal
LA English
CC 56-6 (Nonferrous Metals and Alloys)
AB The morphol. and chem. anal. of the complex phases in cast bronze
contg. 10 Al, 5 Ni, and 5% Fe were investigated using optical and
electron microscopy and energy dispersive anal. The .alpha.-phase,
.beta.-phase, and 4 forms of .kappa. existed in the as-cast
microstructure. Heat treatment lead to pptn. of a further .kappa.
phase which differs in morphol. and chem. compn. to those present in
the as-cast microstructure.
ST bronze cast phase microstructure
IT 63706-44-5
RL: USES (Uses)
(microstructure of cast)
L4 ANSWER 41 OF 61 CA COPYRIGHT 1996 ACS
AN 88:139507 CA
TI Wonominta Block - regional geology and mineralization
AU ***Rose, G.***
CS Geol. Surv. New South Wales, Aust.
SO Monogr. Ser. - Australas. Inst. Min. Metall. (1975), 5(Econ. Geol.
Aust. Papua New Guinea, Vol. 1), 508-10
CODEN: MSAMDR
DT Journal
LA English
CC 53-2 (Mineralogical and Geological Chemistry)
AB The title area consists of the Precambrian sediments of low
metamorphic grade. Au, Cu, and Ag-Pb ore deposits occur in the
area.
ST gold ore deposit Australia; copper ore deposit Australia; silver ore
deposit Australia; lead ore deposit Australia
IT Geology
(of Australia, Wonominta Block)
IT Gold ores
Silver ores
Copper ores, occurrence
Lead ores, occurrence
RL: OCCU (Occurrence)
(of Australia, Wonominta Block)
L4 ANSWER 42 OF 61 CA COPYRIGHT 1996 ACS
AN 85:61358 CA
TI Degradation of steroids: XV. Formation of 9,10-seco-compounds from
4-chlorosubstituted steroids by Nocardia opaca
AU Hoerhold, C.; ***Rose, G.*** ; Hueller, E.; Schubert, K.
CS Zentralinst. Mikrobiol. Exp. Ther., DAW, Jena, E. Ger.
SO J. Steroid Biochem. (1976), 7(3), 199-202
CODEN: JSTBBK
DT Journal
LA German
CC 16-2 (Fermentations)
Section cross-reference(s): 32
AB 4-Chlorotestosterone, the corresponding 17.alpha.-methyl-substituted
steroid, and the compd. with an addnl. double bond in position 1 (I)
have been transformed to 9,10-seco compds. by 9.alpha.-hydroxylation
and 1-dehydrogenation in fermn. cultures of N. opaca. I was
hydrogenated in position 1 to give 4-chloromethyltestosterone. The
metab. of 4-chlorotestosterone could be markedly increased by addn.
of estrone.
ST steroid degrdn Nocardia; chlorotestosterone metab Nocardia
IT Steroids, biological studies
RL: BPR (Biological process); BIOL (Biological study); PROC
(Process)
(metab. of, by Nocardia opaca)
IT Nocardia opaca
(steroid degrdn. by)
IT 5785-58-0 59917-24-7 59917-25-8 59917-26-9 59917-27-0
RL: FORM (Formation, nonpreparative)
(formation of, by Nocardia opaca)
IT 1093-58-9 2446-23-3
RL: BPR (Biological process); BIOL (Biological study); PROC
(Process)
(metab. of, by Nocardia opaca)
L4 ANSWER 43 OF 61 CA COPYRIGHT 1996 ACS
AN 83:148115 CA
TI Anionic polyamide urea urethane ionomers
AU Lorenz, O.; ***Rose, G.***
CS Fachbereich 3-Chem., Fachhochsch. Aachen, Aachen, Ger.
SO Angew. Makromol. Chem. (1975), 45(1), 85-104
CODEN: ANMCBO
DT Journal
LA German
CC 36-3 (Plastics Manufacture and Processing)
AB The title ionomers, i.e. adipic acid-ethylenediamine-hexamethylene
diisocyanate-1,6-hexanediol-neopentyl glycol-pyromellitic
dianhydride polymer [56592-82-6], were prepd. by polymn of
NCO-terminated prepolymers with diamines and dianhydrides. Anal. of
NCO content indicated that 2:1 diamine-dianhydride adducts which
were formed in situ acted as chain-extenders. During prepn. and
storage of the dispersions, excess NCO reacted with H2O with chain
extension, while in the absence of solvent or dispersant reaction
with urea or urethane groups took place. Moduli increased with
increasing concn. of CO2- groups, and phys. crosslinks formed by H
bonding or coulombic forces could be largely removed by swelling
with H2O.
ST ionomer anionic polyurethane; polyamide polyurethane ionomer; urea
polyurethane ionomer; anhydride polyurethane ionomer; pyromellitic
dianhydride ionomer
IT Hydrogen bond
(crosslinking by, of polyurethane ionomers, swelling effect on)
IT Urethane polymers, preparation
RL: SPN (Synthetic preparation); PREP (Preparation)
(ionomers, prepn. and properties of)
IT Crosslinking
(phys., of polyurethane ionomers, swelling effect on)
IT Polyureas
Polyamides, preparation
RL: PREP (Preparation)
(polyurethane-, ionomers)
IT Ionomers
RL: SPN (Synthetic preparation); PREP (Preparation)
(polyurethane-based, prepn. and properties of)
IT 56592-82-6P 56592-83-7P 56592-84-8P
RL: SPN (Synthetic preparation); PREP (Preparation)
(ionomers, prepn. and properties of)
L4 ANSWER 44 OF 61 CA COPYRIGHT 1996 ACS
AN 83:74128 CA
TI Long-chain fatty acyl-CoA synthetase from rat liver microsomes
AU Bar-Tana, J.; ***Rose, G.*** ; Shapiro, B.
CS Hadassah Med. Sch., Hebrew Univ., Jerusalem, Israel
SO Methods Enzymol. (1975), 35, Pt. B, 117-22
CODEN: MENZAU
DT Journal; General Review
LA English
CC 7-0 (Enzymes)
AB A review with 11 refs. on the assay, purifn. and properties of acyl
CoA synthetase of liver microsomes.
ST review acyl CoA synthetase liver
IT Liver, composition
(acyl CoA synthetase of microsome of)
IT Microsome
(acyl CoA synthetase of, of liver)
IT 9013-18-7
RL: BOC (Biological occurrence); BIOL (Biological study); OCCU
(Occurrence)
(of liver microsome)
L4 ANSWER 45 OF 61 CA COPYRIGHT 1996 ACS
AN 82:167160 CA
TI Minimization of construction errors in bent-wire protein models
AU Goldberg, D.; Saliterman, S.; Wetlaufer, D. B.; ***Rose, G.*** ;
Hopkins, Ted E.
CS Med. Sch., Univ. Minnesota, Minneapolis, Minn., USA
SO Biopolymers (1975), 14(3), 633-40
CODEN: BIPMAA
DT Journal
LA English
CC 9-13 (Biochemical Methods)
Section cross-reference(s): 6
AB Two kinds of errors are found in protein models made with the
bent-wire tool of B. Rubin and J. S. Richardson (1972). Global
errors result from the accumulation of many errors too small to
localize, whereas local errors are assignable to particular bends in
the model. The sources of local errors were located and it is shown
how to minimize both kinds of errors.
ST protein conformation model error; bent wire protein model
IT Proteins
RL: PRP (Properties)
(conformation of, bent-wire models for, construction errors in
relation to)
IT Chains, chemical
(conformation of, of proteins, bent-wire models for)
IT Models, physical
(for protein conformation, construction errors in bent-wire)
L4 ANSWER 46 OF 61 CA COPYRIGHT 1996 ACS
AN 80:34689 CA
TI Palmitoyl-coenzyme A synthetase. Isolation of an enzyme-bound
intermediate
AU Bar-Tana, J.; ***Rose, G.*** ; Shapiro, B.
CS Dep. Biochem., Heb. Univ. Hadassah Med. Sch., Jerusalem, Israel
SO Biochem. J. (1973), 135(3), 411-16
CODEN: BIJOAK
DT Journal
LA English
CC 7-4 (Enzymes)
AB Labeling studies showed an enzyme-bound intermediate of the reaction
catalyzed by rat liver microsomal palmitoyl-CoA synthetase (E.C.
6.2.1.3) which contained equimolar amts. of adenylate and fatty acid
moieties. The intermediate was stabilized by 50mM ATP and reacted
with CoA to give palmitoyl-CoA.
ST palmitoyl CoA synthetase intermediate; microsome palmitoyl CoA
synthetase; mechanism palmitoyl CoA synthetase
IT Liver, composition
(palmitoyl coenzyme A synthetase of, reaction intermediate of)
IT 9013-18-7
RL: BIOL (Biological study)
(reaction intermediate of liver microsomal)
L4 ANSWER 47 OF 61 CA COPYRIGHT 1996 ACS
AN 79:103627 CA
TI Microbial hydrogenation of an aromatic system of
17.alpha.-ethinylestradiol
AU Schubert, K.; ***Rose, G.*** ; Hoerhold, Claere
CS Forschungszent. Molekularbiol. Med., Akad. Wiss., Jena, E. Ger.
SO J. Steroid Biochem. (1973), 4(3), 283-8
CODEN: JSTBBK
DT Journal
LA German
CC 16-13 (Fermentations)
AB This is the first report on the enzymic hydrogenation of aromatic
steroids by molds. Aspergillus flavus transformed
17.alpha.-ethynylestradiol (I) to 10.beta.-hydroxy-19-norethisterone
(II). The mold was grown on malt agar slants for 3 days, then for 2
days on a rotary shaker in 100 ml malt water (in 500 ml Florence
flask) at 28.degree., then 10 mg steroid in 0.5 ml acetone was added
as substrate. Fermn. was continued on the shaker for another 2
days. The culture liquid was extd. with CHCl3 and the combined
exts. were evapd. to dryness in vacuo. Identification was by thin
layer chromatog. Under aerobic conds., A. flavus was capable of
hydrogenation and 10.beta.-hydroxylation only on
17.alpha.-methylestradiol, and of hydrogenation without
10.beta.-hydroxylation only on 19-norandrost-1-ene-3,17-dione and
1,4-androstadiene-3,17-dione. There was no action on estradiol,
19-nortestosterone, 3-deoxytestosterone, and norgestrel. Under
anaerobic conds., A. flavus was capable of hydrogenation, but not of
10.beta.-hydroxylation, of ethynylestradiol only. There was no
action on estradiol or norethisterone.
ST ethynylestradiol hydrogenation Aspergillus; steroid hydrogenation
Aspergillus; norethisterone formation Aspergillus
IT Aspergillus flavus
(arom. steroid hydrogenation by)
IT Steroids, biological studies
RL: BIOL (Biological study)
(arom., hydrogenation by Aspergillus)
IT Hydrogenation
(of arom. steroids, by Aspergillus)
IT 1236-00-6
RL: FORM (Formation, nonpreparative)
(formation of, from ethynylestradiol by Aspergillus)
IT 57-63-6
RL: RCT (Reactant)
(hydrogenation of, by Aspergillus)
L4 ANSWER 48 OF 61 CA COPYRIGHT 1996 ACS
AN 78:120845 CA
TI Rat liver microsomal palmitoyl-coenzyme A synthetase. Structural
properties
AU Bar-Tana, J.; ***Rose, G.***
CS Hadassah Med. Sch., Heb. Univ., Jerusalem, Israel
SO Biochem. J. (1973), 131(3), 443-9
CODEN: BIJOAK
DT Journal
LA English
CC 7-5 (Enzymes)
AB Unavailable
ST palmitoyl CoA synthetase liver; phospholipid palmitoyl CoA
synthetase
IT Liver, composition
(acyl coenzyme A synthetase of microsomes of, structure of)
IT Phospholipids
Amino acids, biological studies
RL: BIOL (Biological study)
(of acyl coenzyme A synthetase)
IT 9013-18-7
RL: BIOL (Biological study)
(structure of liver microsomal)
L4 ANSWER 49 OF 61 CA COPYRIGHT 1996 ACS
AN 78:94317 CA
TI Palmitoyl-coenzyme A synthetase. Mechanism of reaction
AU Bar-Tana, J.; ***Rose, G.*** ; Brandes, R.; Shapiro, B.
CS Hadassah Med. Sch., Hebrew Univ., Jerusalem, Israel
SO Biochem. J. (1973), 131(2), 199-209
CODEN: BIJOAK
DT Journal
LA English
CC 7-4 (Enzymes)
AB The mechanism of long-chain fatty acid activation catalyzed by
highly purified microsomal palmitoyl-CoA synthetase (EC 6.2.1.3) was
studied. The kinetics of the overall reaction indicated a Bi Uni
Uni Bi Ping Pong mechanism. 18O was transferred from palmitate-18O
to AMP and palmitoyl-CoA exclusively. An enzyme-bound palmitate
intermediate was formed in the presence of ATP. However,
pulse-labeling expts. with ATP-U-14C, ATP-.gamma.-32P, and
palmitoyl-3H-CoA could not show that the intermediate was definitely
palmitoyl-AMP.
ST palmitoyl CoA synthetase mechanism; kinetics palmitoyl CoA
synthetase
IT Michaelis constant
Kinetics, enzymic
(of acyl coenzyme A synthetase)
IT 9013-18-7
RL: MSC (Miscellaneous); PRP (Properties)
(reaction mechanism of)
L4 ANSWER 50 OF 61 CA COPYRIGHT 1996 ACS
AN 78:13276 CA
TI Microsomal palmitoyl-coenzyme A synthetase from rat liver. Partial
and exchange reactions
AU Bar-Tana, J.; ***Rose, G.*** ; Shapiro, B.
CS Hadassah Med. Sch., Heb. Univ., Jerusalem, Israel
SO Biochem. J. (1972), 129(5), 1101-7
CODEN: BIJOAK
DT Journal
LA English
CC 7-4 (Enzymes)
AB The partial and exchange reactions of long-chain fatty acid
activation were detd. by using purified microsomal long-chain fatty
acyl-CoA synthetase (EC 6.2.1.3). No significant ATP formation from
palmitoyl-AMP (I) and pyrophosphate, nor I-dependent CoA
disappearance was obsd. and no palmitate-dependent
pyrophosphate-32P2-ATP exchange was catalyzed by the pure enzyme.
These reactions were, however, catalyzed by the parent microsomal
fraction at rates similar to the overall rates. Two enzyme
activities must be involved in microsomal acyl-CoA synthesis. The
microsomal partial reactions may reflect activity related to the
enzyme involving bound I as an intermediate, but the second
activity, isolated as the pure enzyme fraction, may comprise
activity catalyzing fatty acid activation in the absence of partial
reactions.
ST palmitoyl CoA synthetase liver; microsome palmitoyl CoA synthetase;
fatty acyl CoA synthetase; Michaelis const synthetase; kinetics
palmitoyl CoA synthetase
IT Michaelis constant
(of palmitoyl coenzyme A synthetase)
IT Kinetics, enzymic
(of palmitoyl coenzyme A synthetase, partial and exchange
reactions in)
IT 9013-18-7
RL: PRP (Properties)
(reaction kinetics of, partial and exchange reactions in)
L4 ANSWER 51 OF 61 CA COPYRIGHT 1996 ACS
AN 76:137736 CA
TI Determination of oxygen-18 content of phosphate compounds. Novel
method
AU Bar-Tana, J.; Ben-Zeev, O.; ***Rose, G.*** ; Deutsh, J.
CS Hadassah Med. Sch., Heb. Univ., Jerusalem, Israel
SO Biochim. Biophys. Acta (1972), 264(1), 214-19
CODEN: BBACAQ
DT Journal
LA English
CC 9 (Biochemical Methods)
AB Silylation of phosphate and phosphate-contg. compds. provides a
suitable means for the direct measurement of the 18O content of
phosphate compds. The silylation procedure is described for 2 model
systems: ATP hydrolysis by H218O and 18O transfer from
HOAc-carboxy-18O to AMP. An evaluation of the suggested procedure
is presented.
ST phosphate oxygen isotope detn
IT Phosphates, analysis
RL: ANST (Analytical study)
(oxygen-18 detn. in, by silylation and mass spectroscopy)
IT 9000-95-7
RL: ANST (Analytical study)
(ATP hydrolysis by, detn. of oxygen-18 transfer in)
IT 14797-71-8, analysis
RL: ANT (Analyte); ANST (Analytical study)
(detn. of, in phosphates by silylation and mass spectroscopy)
IT 56-65-5, biological studies
RL: RCT (Reactant)
(hydrolysis of, by apyrase, detn. of oxygen-18 transfer in)
IT 9012-31-1
RL: ANST (Analytical study)
(oxygen-18 transfer to AMP from acetic acid by, detn. of)
IT 61-19-8, biological studies
RL: BIOL (Biological study)
(oxygen-18 transfer to, from acetic acid by acetyl coenzyme A
synthetase, detn. of)
L4 ANSWER 52 OF 61 CA COPYRIGHT 1996 ACS
AN 76:94924 CA
TI Metabolism of steroid drugs. VIII. Structure-metabolism relations
in the microbiol of hydrogenation various substituted testosterone
derivatives
AU Schubert, K.; Schlegel, J.; Groh, H.; ***Rose, G.*** ; Hoerhold,
Claere
CS Zentralinst. Mikrobiol. Exp. Ther., Dtsch. Akad. Wiss. Berlin,
Berlin, Ger.
SO Endokrinologie (1972), 59(1), 99-114
CODEN: ENDKAC
DT Journal
LA German
CC 2 (Hormone Pharmacology)
AB Metabolism of the androgen-anabolic steroids, testosterone
[58-22-0], methyltestosterone [58-18-4], 1-dehydromethyltestosterone
[72-63-9], 4-chloromethyltestosterone [5785-58-0], and
1-dehydro-4-chloromethyltestosterone [34417-59-9], by Aspergillus
flavus, Clostidium paraputrificum, and Rhodotorula glutinis was
investigated as a possible model for the hydroxylation and
hydrogenation pathways in mammalian steroid metabolism.
Testosterone was hydroxylated in the B ring after oxidn. to
androstenedione by A. flavus, whereas 4-chloro-17.alpha.-
methyltestosterone and 1-dehydromethyltestosterone were metabolized
to 15-hydroxy compds. The 15-hydroxylation was a function of the
17.alpha.-methyl group, whereas a chloro substituent or a double
bond in ring A detd. the stereospecificity (15-.alpha. or
15-.beta.). The stereospecificity of the 3.alpha.-OH/5.beta.-H-
hydrogenase of C. paraputrificum was observed with all substrates.
1-Dehydro-4-chloro-17.alpha.-methyltestosterone was metabolized to a
deriv. with a 1-en-3.alpha.-OH-allyl structure in contrast to
1-dehydro-17.alpha.-methyltestosterone which gave the
3.alpha./5.beta.-hexahydro product. The R. glutinis metabolized
testosterone and 17.alpha.-methyltestosterone to
3.alpha.-OH/5.alpha.-H and 3.beta.-OH/5.alpha.-H derivs.
4-Chloro-17.alpha.-methyltestosterone was incompletely metabolized.
No hydrogenation products were formed from 1-dehydro-17.alpha.-
methyltestosterone, but from 1-dehydro-4-chloro-17.alpha.-
methyltestosterone a 1-en-3.beta.-OH/5.alpha.-H-allyl deriv. was
isolated.
ST testosterone metab microbe; Aspergillus testosterone metab;
Clostridium testosterone metab; Rhodotorula testosterone metab
IT Aspergillus flavus
Clostridium paraputrificum
Rhodotorula glutinis
(testosterone derivs. metabolism by)
IT 35937-37-2
RL: FORM (Formation, nonpreparative)
(formation of, from chloromethyltestosterone, by Aspergillus
flavus)
IT 35937-40-7 35937-41-8
RL: FORM (Formation, nonpreparative)
(formation of, from chloromethyltestosterone, by Rhodotorula
glutinis)
IT 27471-86-9 27471-87-0
RL: FORM (Formation, nonpreparative)
(formation of, from dehydrochloromethyltestosterone)
IT 27471-88-1 29834-97-7
RL: FORM (Formation, nonpreparative)
(formation of, from dehydrochloromethyltestosterone, by
Clostridium paraputrificans)
IT 27471-90-5 27471-91-6
RL: FORM (Formation, nonpreparative)
(formation of, from dehydrochloromethyltestosterone, by
Rhodotorula glutinis)
IT 35937-38-3
RL: FORM (Formation, nonpreparative)
(formation of, from dehydromethyltestosterone, by Clostridium
paraputrificans)
IT 35937-36-1 36018-59-4
RL: FORM (Formation, nonpreparative)
(formation of, from dehydrotestosterone, by Aspergillus flavus)
IT 641-82-7
RL: FORM (Formation, nonpreparative)
(formation of, from methyltestosterone by Rhodotorulia glutinis)
IT 13096-49-6 35937-34-9 35937-35-0
RL: FORM (Formation, nonpreparative)
(formation of, from methyltestosterone, by Aspergillus flavus)
IT 641-83-8
RL: FORM (Formation, nonpreparative)
(formation of, from methyltestosterone, by Rhodotorula glutinis)
IT 4085-03-4
RL: FORM (Formation, nonpreparative)
(formation of, from testosterone derivs., by Clostridium
paraputrificans)
IT 62-84-0 63-00-3 63-05-8 4416-57-3
RL: FORM (Formation, nonpreparative)
(formation of, from testosterone, by Aspergillus flavus)
IT 1851-23-6
RL: FORM (Formation, nonpreparative)
(formation of, from testosterone, by Clostridium paraputrificum)
IT 571-20-0 1852-53-5
RL: FORM (Formation, nonpreparative)
(formation of, from testosterone, by Rhodotorula glutinis)
IT 35937-39-4
RL: BIOL (Biological study)
(formaton of, from chloromethyltestosterone, by Clostridium
paraputrificans)
IT 58-18-4 58-22-0 72-63-9 2446-23-3 5785-58-0
RL: BPR (Biological process); BIOL (Biological study); PROC
(Process)
(metabolism of, by microorganisms)
IT 35937-42-9P
RL: SPN (Synthetic preparation); PREP (Preparation)
(prepn. of)
L4 ANSWER 53 OF 61 CA COPYRIGHT 1996 ACS
AN 75:15328 CA
TI Purification and properties of microsomal palmitoyl-coenzyme A
synthetase
AU Bar-Tana, J.; ***Rose, G.*** ; Shapiro, B.
CS Hadassah Med. Sch., Heb. Univ., Jerusalem, Israel
SO Biochem. J. (1971), 122(3), 353-62
CODEN: BIJOAK
DT Journal
LA English
CC 3 (Enzymes)
AB Palmitoyl-CoA synthetase was isolated and purified from rat liver
microsomes. The lipid components were removed by treatment of the
freeze-dried microsomal prepns. with org. solvents before
dissolution of the particles by detergent. A min. concn. of
detergents was also maintained throughtout the purification
procedure. The procedure may facilitate the isolation of other
membrane enzymes that have resisted purification. The enzyme had a
pH optimum of 8-9. The enzyme required Mg2+, ATP, CoA, and the
presence of detergent for activity. Palmitate was the best
substrate for the enzyme, but laurate, myristate, stearate, and
linoleate were also good substrates. Km Values were 42, 22, 11, 15,
15, and 25 .mu.M for palmitate, myristate, laurate, stearate,
oleate, and linoleate, resp.
ST palmitoyl CoA synthetase purifn props; fatty acyl CoA synthetase
purifn
IT Synthetases, acyl coenzyme A
(of liver, purification of)
IT Michaelis constant
(of palmitoyl coenzyme A synthetase)
IT Liver, composition
(palmitoyl coenzyme A synthetase of microsomes of)
IT 1763-10-6 14000-31-8
RL: RCT (Reactant)
(reaction of, with palmitoyl coenzyme A synthetase, Michaelis
const. for)
IT 56-65-5, reactions 57-10-3, reactions 57-11-4, reactions
60-33-3, reactions 61-19-8, reactions 85-61-0, reactions
112-80-1, reactions 143-07-7, reactions 544-63-8, reactions
RL: RCT (Reactant)
(with palmitoyl coenzyme A synthetase, Michaelis const. for)
L4 ANSWER 54 OF 61 CA COPYRIGHT 1996 ACS
AN 74:33697 CA
TI Morphology of winter anomaly of absorption
AU Dieminger, W.; ***Rose, G.*** ; Schwentek, H.; Widdel, H. U.
CS Max-Planck-Inst. Aeron., Lindau Harz, Ger.
SO Proc. Int. Space Sci. Symp. (1967), Volume Date 1966, 7(Vol. 1),
228-39
CODEN: PSPSAE
DT Journal
LA English
CC 53 (Mineralogical and Geological Chemistry)
AB The characteristics of the winter anomaly of ionospheric absorption
are summarized.
ST winter anomaly ionospheric absorption; ionospheric absorption winter
anomaly; absorption ionospheric winter anomaly
IT Ionosphere
(absorption in, winter anomaly of)
L4 ANSWER 55 OF 61 CA COPYRIGHT 1996 ACS
AN 71:57814 CA
TI Sterols in bacteria
AU Schubert, Kurt; ***Rose, G.*** ; Hoerhold, Claere
CS Deut. Akad. Wiss. Berlin, Jena, Ger.
SO Abh. Deut. Akad. Wiss. Berlin, Kl. Med. (1969), Volume Date 1968,
No. 2, 53-6
CODEN: ADWMAX
DT Journal
LA English
CC 8 (Microbial Biochemistry)
AB The sterol (I) content of several strains of bacteria has been
investigated. Escherichia coli contains 7, Azotobacter chroococcum
6, and Streptomyces olivaceus one I. For the detn. of mass nos. and
quant. estn., the method of mass mol. spectrometry with ionization
by addn. of neg. ions was used. The quantities of I in bacteria are
small. The isolation and identification of I show that bacteria may
not differ from more highly developed organisms in respect to the
presence of I. The bacteria synthesize and also degrade I.
ST sterols bacteria; bacteria sterols; synthesis sterols bacteria
IT Steroids, biological studies
RL: BIOL (Biological study)
(hydroxy, in bacteria)
IT Bacteria
(sterols in)
L4 ANSWER 56 OF 61 CA COPYRIGHT 1996 ACS
AN 69:83526 CA
TI Medium-chain fatty acyl coenzyme A synthetase. Enzyme fraction II:
mechanism of reaction and specific properties
AU Bar-Tana, J.; ***Rose, G.***
CS Hadassah Med. Sch., Hebrew Univ., Jerusalem, Israel
SO Biochem. J. (1968), 109(2), 283-92
CODEN: BIJOAK
DT Journal
LA English
CC 3 (Enzymes)
AB The mechanism of reaction of fatty acyl CoA synthesis catalyzed by
fatty acyl CoA synthetase from ox liver (fraction II; Bar-Tana,
Rose, and Shapiro (1968)) was investigated by a kinetic study of CoA
disappearance dependent on butyrate plus ATP or butyryl-AMP (overall
and partial reaction b, resp.). Contrary to findings with another
enzyme (fraction I), a Bi Uni Uni Bi Ping Pong mechanism (Cleland
(1963)) corresponding to Berg's (1956) scheme of reaction was
eliminated and an ordered Ter Ter mechanism with an A-C-B (standing
for ATP, CoA and butyrate, resp.) sequence of substrate entry for
the overall reaction was established for fraction II. Partial
reaction b was found to follow the "Iso-Theorell-Chance" mechanism.
Also, in contrast with results obtained with fraction I, no
allosteric properties could be demonstrated with fraction II.
ST fatty acl CoA synthetase; mechanism acyl CoA synthetase; acyl CoA
synthetase mechanism; kinetics acyl CoA synthetase
IT Kinetics, enzymic
(of acyl coenzyme A synthetase)
IT Synthetases, acyl coenzyme A
(reaction mechanism of)
L4 ANSWER 57 OF 61 CA COPYRIGHT 1996 ACS
AN 69:83525 CA
TI Medium-chain fatty acyl coenzyme A synthetase. Enzyme fraction I:
mechanism of reaction and allosteric properties
AU Bar-Tana, J.; ***Rose, G.***
CS Hadassah Med. Sch., Hebrew Univ., Jerusalem, Israel
SO Biochem. J. (1968), 109(2), 275-82
CODEN: BIJOAK
DT Journal
LA English
CC 3 (Enzymes)
AB The mechanism of butyrate activation catalyzed by an enzyme fraction
derived from ox liver particles (fraction I; Bar-Tana, Rose, and
Shapiro (1968)) was studied by an anal. of the initial-velocity
pattern of the overall reaction and found to conform to the Bi Uni
Uni Bi Ping Pong model (Cleland (1963)) in agreement with the
reaction scheme proposed by Berg (1956). A homotropic co-operative
effect was exerted by CoA on fraction I, whereas ATP and AMP
functioned as heterotropic co-operative ligands with respect to
butyryl-AMP-dependent CoA disappearance. On the other hand, PPi and
butyryl CoA showed antagonistic heterotropic effects when tested
under similar conditions. With respect to the overall reaction CoA
and ATP could be shown to function as co-operative homotropic
modifiers. Two interchangeable conformational states of the enzyme
are therefore presumed to exist, state R, having a higher affinity
for CoA and ATP and thus preferentially catalyzing
butyryl-AMP-dependent CoA disappearance (partial reaction b), and
state T, favored by the presence of PPi, catalyzing the formation of
ATP from butyryl-AMP and PPi (partial reaction a) with greater
efficiency. These findings serve to explain the opposite effects of
ATP on the partial reactions, as well as the inhibition by CoA and
ATP of ATP formation (reaction a) and by PPi of the
butyryl-AMP-dependent CoA disappearance (reaction b) (Bar-Tana, et
al. (1968)). The possible analogy of these observations to amino
acid-activating and other similar systems is discussed.
ST acyl CoA synthetase mechanism; mechanism acyl CoA synthetase;
allosteric props CoA synthetase; CoA synthetase allosteric props
IT Kinetics, enzymic
(of acyl coenzyme A synthetase)
IT Synthetases, acyl coenzyme A
(reaction mechanism and allosteric properties of)
L4 ANSWER 58 OF 61 CA COPYRIGHT 1996 ACS
AN 69:83524 CA
TI Medium-chain fatty acyl coenzyme A synthetase. Purification and
properties
AU Bar-Tana, J.; ***Rose, G.*** ; Shapiro, B.
CS Hadassah Med. Sch., Hebrew Univ., Jerusalem, Israel
SO Biochem. J. (1968), 109(2), 269-74
CODEN: BIJOAK
DT Journal
LA English
CC 3 (Enzymes)
AB Medium-chain fatty acyl CoA synthetase (EC 6.2.1.2) was isolated by
the method of Mahler, Wakil, and Bock (1953) and the enzyme activity
detd. by the disappearance of CoA in the presence of butyrate and
ATP or of butyryl-AMP, as well as by ATP formation from butyryl-AMP
and PPi. Preincubation of the enzyme with CoA and ATP alone or
together, followed by the removal of these substrates by gel
filtration, caused a marked inhibition of ATP formation, contrary to
results previously obtained with palmitoyl CoA synthetase. The
effect of ATP on butyryl-AMP-dependent CoA disappearance was
inconsistent. Low concns. of ATP (0.1-0.5 mM) always caused
inhibition, whereas higher concns. (5-10 mM) activated in some
enzyme prepns. and inhibited in others. This inconsistency was
shown to be due to the presence of 2 enzyme fractions. Both
fractions had similar activities when assayed by the butyryl-AMP- or
butyrate-plus-ATP-dependent CoA disappearance. However, fraction I
was activated by ATP as measured by butyryl-AMP-dependent CoA
disappearance whereas fraction II was inhibited by it. Fraction I
also catalyzed ATP formation from butyryl-AMP and PPi whereas
fraction II was lacking in such activity. The relation of these
observations with respect to other known mechanisms of fatty
acid-activating systems is discussed.
ST fatty acyl CoA synthetase; acyl CoA synthetase; CoA synthetase
purifn
IT Kinetics, enzymic
(of acyl-coenzyme A synthetase)
IT Synthetases, acyl coenzyme A
(purification and properties of)
IT 56-65-5, biological studies
RL: BIOL (Biological study)
(acyl-coenzyme A synthetase response to)
L4 ANSWER 59 OF 61 CA COPYRIGHT 1996 ACS
AN 69:69985 CA
TI The effect of capillary liquid on the force of adhesion between
spherical solid particles. Comment
AU Gillespie, T.; ***Rose, G. D.***
CS Edgar C. Britton Res. Lab., Dow Chem. Co., Midland, Mich., USA
SO J. Colloid Interface Sci. (1968), 26(2), 246-7
CODEN: JCISA5
DT Journal
LA English
CC 66 (Surface Chemistry and Colloids)
AB Data are presented to refute the criticism of Gilespie and Settineri
(ibid., 1967, 24, 199) on Fisher's theory. Modifying the procedure
for cleaning the beads altered the results so that smaller forces at
high surface-tension values were obtained than those reported.
ST adhesion solids effect capillary liq; solids adhesion effect
capillary liq
IT Particles
(adhesion between spherical solid, capillarity effect on,
Fisher's theory in relation to)
IT Adhesion
(between spherical solid particles, capillarity effect on,
Fisher's theory in relation to)
IT Capillarity
(effect on adhesion forces between spherical solid particles,
Fisher's theory in relation to)
L4 ANSWER 60 OF 61 CA COPYRIGHT 1996 ACS
AN 69:49901 CA
TI Occurrence of sterols in bacteria
AU Schubert, K.; ***Rose, G.*** ; Wachtel, H.; Hoerhold, C.;
Ikekawa, N.
CS Deut. Akad. Wiss. Berlin, Jena, Ger.
SO Eur. J. Biochem. (1968), 5(2), 246-51
CODEN: EJBCAI
DT Journal
LA German
CC 8 (Microbial Biochemistry)
AB Investigations concerning sterols were made in strain of each of 9
species of bacteria and 1 representative of the basidiomycetes
through adsorption chromatog., gas chromatog., and mass spectrometry
as well as uv and ir spectroscopy. Three strains contained sterols
in quantities from 0.0004 to 0.01% of the dry wt. In Azotobacter
chroococcum 6 sterols were demonstrated. In 6 strains sterols were
not detectable. The limit of detectability at present is at 0.0001%
sterol related to 100 g. dry cells. From the ext. of Aerobacter
cloacae, which contained no sterol, a C16-hydroxyketone was
isolated.
ST sterol compn bacteria; Azotobacter sterol compn; Aerobacter sterol
compn; basidiomycetes chromatog sterols
IT Azotobacter
(chroococcum, sterols of)
IT Steroids, biological studies
RL: BIOL (Biological study)
(hydroxy, of bacteria)
IT Bacteria
(sterols of)
IT Ergost-7-en-3.beta.-ol
RL: BIOL (Biological study)
(in Azotobacter chroococcum)
IT 57-87-4 79-63-0 5241-24-7 7448-02-4 17608-76-3
RL: BIOL (Biological study)
(in Azotobacter chroococcum)
L4 ANSWER 61 OF 61 CA COPYRIGHT 1996 ACS
AN 69:30393 CA
TI Gas transport through supported Langmuir-Blodgett multilayers
AU ***Rose, G. D.*** ; Quinn, J. A.
CS Univ. of Illinois, Urbana, Ill., USA
SO J. Colloid Interface Sci. (1968), 27(2), 193-207
CODEN: JCISA5
DT Journal
LA English
CC 66 (Surface Chemistry and Colloids)
AB Mass transfer coeffs. for Langmuir-Blodgett multilayers deposited
onto permeable support films were measured for 3 gases: CO2, N, and
He. For stearate multilayers varying in thickness from 48 to 4
deposited layers (1200 to 100 A.), the permeabilities
[in(cc.(STP)-cm.)/(cm.2-sec.-cm. Hg)] range from 4 to 20 .times.
10-10 for CO2, from 1 to 8 .times. 10-10 for He, and from 0.5 to 2
.times. 10-10 for N. The measured permeabilities were essentially
independent of the surface pressure at which the monolayers were
deposited for surface pressures between 9 and 29 dynes/cm. Tracer
techniques were used to observe both the regularity and concn. of
the deposited layers. Results were also obtained for oleic acid and
3.beta.-cholestanol. The cholestanol permeabilities were comparable
to those of stearic acid whereas the oleic acid values were at least
an order of magnitude larger. The results are compared to
permeabilities of polymeric films and monolayers on aq. substrates.
ST permeable films; films permeable; gas transport; Langmuir Blodgett
multilayers
IT Mass transfer
(in permeation of gases through supported multilayers)
IT Permeation
(of gases, through supported multilayers)
IT 57-11-4, properties 80-97-7 112-80-1, properties
RL: PRP (Properties)
(permeation by supported multilayers of, of gases)
IT 124-38-9, properties 7440-59-7, properties 7727-37-9, properties
RL: PRP (Properties)
(permeation of, through supported multilayers)
=> ^Y
=> log Y
COST IN U.S. DOLLARS SINCE FILE TOTAL
ENTRY SESSION
FULL ESTIMATED COST 205.45 205.65
DISCOUNT AMOUNTS (FOR QUALIFYING ACCOUNTS) SINCE FILE TOTAL
ENTRY SESSION
CA SUBSCRIBER PRICE -46.64 -46.64
STN INTERNATIONAL LOGOFF AT 17:38:30 ON 02 JUL 96