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  • Protein Conformation
  • American Association for the Advancement of Science (AAAS)  (40)
  • 1980-1984  (40)
Collection
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Publisher
  • American Association for the Advancement of Science (AAAS)  (40)
Years
Year
  • 1
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    Cyclic AMP receptor protein: role in transcription activation (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-05-25
    Description: The structure of this pleiotropic activator of gene transcription in bacteria and its interaction sites at promoter DNA's as well as the role of this protein in the RNA polymerase-promoter interactions are reviewed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Crombrugghe, B -- Busby, S -- Buc, H -- New York, N.Y. -- Science. 1984 May 25;224(4651):831-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6372090" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallography ; DNA, Bacterial/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Galactose/genetics ; *Gene Expression Regulation ; Lac Operon ; Operon ; Protein Conformation ; Receptors, Cyclic AMP/*physiology ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Amphiphilic secondary structure: design of peptide hormones (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-20
    Description: Peptide synthesis can be used for elucidating the roles of secondary structures in the specificity of hormones, antigens, and toxins. Intermediate sized peptides with these activities assume amphiphilic secondary structures in the presence of membranes. When models are designed to optimize the amphiphilicity of the secondary structure, stronger interactions can be observed with the synthetic peptides than with the naturally occurring analogs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, E T -- Kezdy, F J -- HL-18577/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):249-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322295" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoprotein A-I ; Apolipoproteins ; Binding Sites ; Calcitonin ; Chemical Phenomena ; Chemistry ; Corticotropin-Releasing Hormone ; Endorphins ; Glucagon ; Growth Hormone-Releasing Hormone ; *Hormones/pharmacology ; Lipoproteins, HDL ; Melitten ; Models, Structural ; *Peptides/chemical synthesis/metabolism/pharmacology ; Protein Conformation ; Structure-Activity Relationship ; beta-Endorphin
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  • 3
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    Nucleosome reconstruction via phosphorus mapping (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-23
    Description: Electron spectroscopic imaging was combined with reconstruction algorithms to derive the three-dimensional structure of the nucleosome core particle to a resolution of 1.5 nanometers. Images of phosphorus distributions within individual nucleosomes were interpreted as projections of a supercoil of DNA. These were used to orient the corresponding individual nucleosome images, making it possible to reconstruct the entire nucleosome in three dimensions. The structure is consistent with known biochemical and biophysical data and explains site-specific nuclease sensitivity, although differing in part with other nucleosome models.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harauz, G -- Ottensmeyer, F P -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):936-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6505674" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/analysis ; Deoxyribonucleoproteins/analysis ; Histones/analysis ; Microscopy, Electron/methods ; Models, Structural ; Nucleic Acid Conformation ; Nucleosomes/*ultrastructure ; Protein Conformation ; Spectrum Analysis/methods
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  • 4
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    Inhibition of collagen fibril formation in vitro and subsequent cross-linking by glucose (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-28
    Description: Glucose inhibits collagen fibril formation in vitro. A linear dose response was observed, with half-maximum inhibition of fibril formation occurring at 50 mM glucose. Nonfibrillar collagen cannot be cross-linked by lysyl oxidase, an enzyme that catalyzes the initial cross-linking reaction. The degree of decreased fibril formation correlated with the loss of ability of the collagen to serve as a substrate for lysyl oxidase. Collagen that is not cross-linked is unstable and more susceptible to collagenolytic attack. Interference with collagen cross-linking and more rapid degradation may explain the decreased amounts of interstitial collagen and the poor healing of wounds associated with diabetes mellitus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lien, Y H -- Stern, R -- Fu, J C -- Siegel, R C -- New York, N.Y. -- Science. 1984 Sep 28;225(4669):1489-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6147899" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Collagen/*metabolism ; Diabetes Mellitus/metabolism ; Diabetes Mellitus, Experimental/metabolism ; Elastin/metabolism ; Glucose/*pharmacology ; Humans ; In Vitro Techniques ; Macromolecular Substances ; Protein Conformation ; Protein-Lysine 6-Oxidase/metabolism ; Rats
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  • 5
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    Message transmission: receptor controlled adenylate cyclase system (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-21
    Description: The adenylate cyclase system is composed of an activating hormone or neurotransmitter (H), its receptor (R), the guanosine triphosphate (GTP) binding protein (Gs), and the catalytic unit (C). The activation of the receptor R involves a transient change in conformation, from a loose binding of the neurotransmitter H to an extremely tight interaction, termed locking. The system is regulated in the activation steps and also by three deactivation processes. A guanosine triphosphatase activity is built into the Gs protein so that the active GsGTP has only a limited lifetime during which it is able to activate C. In addition, the continued occupation of R by H causes desensitization of R. Finally, there are inhibitory receptors, such as alpha-adrenergic and opiate receptors, which inhibit the adenylate cyclase by way of a specific GTP binding protein (Gi). Yet to be determined are the conformational transformations of pure R on binding of an agonist or a partial agonist; the genes that code for the many different receptors that activate the adenylate cyclase, and the possibility that the G components interact with systems in the cell other than the adenylate cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schramm, M -- Selinger, Z -- AM10451/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1350-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6147897" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/*metabolism ; Animals ; Cyclic AMP/*physiology ; Enzyme Activation ; GTP Phosphohydrolases/metabolism ; GTP-Binding Proteins ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Guanylyl Imidodiphosphate/metabolism ; Membrane Lipids/physiology ; Neurotransmitter Agents/physiology ; Protein Conformation ; Receptors, Cell Surface/metabolism ; *Synaptic Transmission
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  • 6
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    Acetylcholine receptor: an allosteric protein (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-21
    Description: The nicotine receptor for the neurotransmitter acetylcholine is an allosteric protein composed of four different subunits assembled in a transmembrane pentamer alpha 2 beta gamma delta. The protein carries two acetylcholine sites at the level of the alpha subunits and contains the ion channel. The complete sequence of the four subunits is known. The membrane-bound protein undergoes conformational transitions that regulate the opening of the ion channel and are affected by various categories of pharmacologically active ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Changeux, J P -- Devillers-Thiery, A -- Chemouilli, P -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1335-45.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6382611" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/analysis ; Electric Organ/metabolism ; Electrophorus ; Macromolecular Substances ; Protein Conformation ; *Receptors, Nicotinic/genetics/metabolism ; Torpedo
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  • 7
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    Homologies between signal transducing G proteins and ras gene products (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-16
    Description: The guanosine triphosphate-binding proteins (G proteins) found in a variety of tissues transduce signals generated by ligand binding to cell surface receptors into changes in intracellular metabolism. Amino acid sequences of peptides prepared by partial proteolysis of the alpha subunit of a bovine brain G protein and the alpha subunit of rod outer-segment transducin were determined. The two proteins show regions of sequence identity as well as regions of diversity. A portion of the amino-terminal peptide sequence of each protein is highly homologous with the corresponding region in the ras protein (a protooncogene product). These similarities suggest that G proteins and ras proteins may have analogous functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, J B -- Simon, M I -- Teplow, D B -- Robishaw, J D -- Gilman, A G -- GM 09731-02/GM/NIGMS NIH HHS/ -- NS 18153/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):860-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6436980" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; GTP-Binding Proteins/*metabolism ; Neoplasm Proteins/*metabolism ; Oncogenes ; Protein Conformation ; Proto-Oncogene Proteins p21(ras) ; Transduction, Genetic
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  • 8
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    Pigment gene scrutinized (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-10-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1984 Oct 5;226(4670):35.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6236555" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cattle ; Eye Proteins/genetics ; *Genes ; Humans ; Photoreceptor Cells/analysis ; Protein Conformation ; Retinal Pigments/*genetics ; Rhodopsin/analysis/*genetics ; Rod Opsins
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  • 9
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    Evolution of proteolytic enzymes (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-27
    Description: Proteolytic enzymes have many physiological functions, ranging from generalized protein digestion to more specific regulated processes such as the activation of zymogens, blood coagulation and the lysis of fibrin clots, the release of hormones and pharmacologically active peptides from precursor proteins, and the transport of secretory proteins across membranes. They are present in all forms of living organisms. Comparisons of amino acid sequences, three-dimensional structures, and enzymatic reaction mechanisms of proteases indicate that there are distinct families of these proteins. Changes in molecular structure and function have accompanied the evolution of proteolytic enzymes and their inhibitors, each having relatively simple roles in primitive organisms and more diverse and more complex functions in higher organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neurath, H -- GM-15731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):350-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6369538" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; *Biological Evolution ; Blood Coagulation ; Chemistry, Physical ; Enzyme Activation ; Enzyme Precursors/metabolism ; Genes ; Humans ; Mutation ; *Peptide Hydrolases/analysis/genetics/metabolism ; Peptides/metabolism ; Physicochemical Phenomena ; Protease Inhibitors/analysis/metabolism ; Protein Conformation ; Protein Sorting Signals ; Substrate Specificity
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  • 10
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    Spectrographic representation of globular protein breathing motions (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-13
    Description: Two useful ways of describing the frequency composition of the breathing motions of globular proteins are the spectrogram and three-dimensional power spectrum, representations similar to those frequently used in speech analysis. In this report "low-frequency" vibrations of globular proteins, corresponding to the collective oscillations of atoms from many different residues, are considered. Radii of gyration fluctuations provide a sensitive way to characterize such concerted motions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pickover, C A -- New York, N.Y. -- Science. 1984 Jan 13;223(4632):181-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6691144" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Physicochemical Phenomena ; Protein Conformation ; Spectrum Analysis ; *Trypsin Inhibitors
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  • 11
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    The molecular structure of a DNA-triostin A complex (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-14
    Description: The molecular structure of triostin A, a cyclic octadepsipeptide antibiotic, has been solved complexed to a DNA double helical fragment with the sequence CGTACG (C, cytosine; G, guanine; T, thymine; A, adenine). The two planar quinoxaline rings of triostin A bis intercalate on the minor groove of the DNA double helix surrounding the CG base pairs at either end. The alanine residues form hydrogen bonds to the guanines. Base stacking in the DNA is perturbed, and the major binding interaction involves a large number of van der Waals contacts between the peptides and the nucleic acid. The adenine residues in the center are in the syn conformation and are paired to thymine through Hoogsteen base pairing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A H -- Ughetto, G -- Quigley, G J -- Hakoshima, T -- van der Marel, G A -- van Boom, J H -- Rich, A -- New York, N.Y. -- Science. 1984 Sep 14;225(4667):1115-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474168" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; DNA/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; Quinoxalines/metabolism
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  • 12
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    Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-12-14
    Description: Few and limited amino acid sequence homologies have been found among eight bacterial aminoacyl transfer RNA (tRNA) synthetases whose primary structures are known. The entire 939-amino acid primary structure of Escherichia coli isoleucyl-tRNA synthetase is now reported. In a sequence of 11 consecutive amino acids matching a sequence in E. coli methionyl-tRNA synthetase, there are ten identical residues and one conservative change. This is the strongest homology recorded between any two aminoacyl tRNA synthetases. This part of the methionine enzyme's three-dimensional structure has been determined, and it occurs in a mononucleotide binding fold; a close three-dimensional structural homology of this part of the enzyme with Bacillus stearothermophilus tyrosyl-tRNA synthetase has also been reported. The three synthetases probably fold identically in this region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Webster, T -- Tsai, H -- Kula, M -- Mackie, G A -- Schimmel, P -- GM15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Dec 14;226(4680):1315-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6390679" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Amino Acyl-tRNA Synthetases ; Escherichia coli/enzymology ; Geobacillus stearothermophilus/enzymology ; Isoleucine-tRNA Ligase ; Methionine-tRNA Ligase ; Protein Conformation
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  • 13
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    Splice junctions: association with variation in protein structure (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-06-10
    Description: A comparison between eukaryotic gene sequences and protein sequences of homologous enzymes from bacterial and mammalian organisms shows that intron-exon junctions frequently coincide with variable surface loops of the protein structures. The altered surface structures can account for functional differences among the members of a family. Sliding of the intron-exon junctions may constitute one mechanism for generating length polymorphisms and divergent sequences found in protein families. Since intron-exon junctions map to protein surfaces, the alterations mediated by sliding of these junctions can be effected without disrupting the stability of the protein core.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craik, C S -- Rutter, W J -- Fletterick, R -- AM21344/AM/NIADDK NIH HHS/ -- AM26081/AM/NIADDK NIH HHS/ -- GM28520/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1125-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344214" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins ; Base Sequence ; Biological Evolution ; DNA/genetics ; Endopeptidases/genetics ; Eukaryotic Cells/metabolism ; Genes ; Genes, Bacterial ; Protein Conformation ; Proteins/*genetics ; *Serine Endopeptidases ; Tetrahydrofolate Dehydrogenase/genetics
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  • 14
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    Monoclonal antibodies reveal the structural basis of antibody diversity (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-11-18
    Description: Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teillaud, J L -- Desaymard, C -- Giusti, A M -- Haseltine, B -- Pollock, R R -- Yelton, D E -- Zack, D J -- Scharff, M D -- 5T32GM7288/GM/NIGMS NIH HHS/ -- AI05231/AI/NIAID NIH HHS/ -- AI10702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):721-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356353" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/genetics/*immunology ; *Antibody Diversity ; Antibody Specificity ; Genes ; Hybridomas/immunology ; Immunoglobulin Idiotypes/immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Mutation ; Protein Conformation ; Structure-Activity Relationship
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  • 15
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    Protein engineering (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-02-11
    Description: The prospects for protein engineering, including the roles of x-ray crystallography, chemical synthesis of DNA, and computer modelling of protein structure and folding, are discussed. It is now possible to attempt to modify many different properties of proteins by combining information on crystal structure and protein chemistry with artificial gene synthesis. Such techniques offer the potential for altering protein structure and function in ways not possible by any other method.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ulmer, K M -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):666-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6572017" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Crystallography ; Genes ; *Genetic Engineering ; Models, Molecular ; Molecular Biology/trends ; Protein Conformation ; Proteins/*genetics ; X-Ray Diffraction
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  • 16
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    Waterlogged molecules (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-12-09
    Description: Measurements of vapor pressures over their aqueous solutions indicate that organic compounds show profound differences in hydrophilic character. These differences are of such magnitude as to suggest an important role for changing solvation in determining free energy changes associated with metabolic transformations in water, and in governing structural equilibria of proteins and other large molecules in water. When two or more functional groups are present within the same solute molecule, their combined effects on its free energy of solvation are commonly additive. Striking departures from additivity, observed in certain cases, indicate the existence of special interactions between different parts of a solute molecule and the water that surrounds it. Similar considerations presumably apply to activated intermediates in the interconversion of biological materials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolfenden, R -- GM 18325/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Dec 9;222(4628):1087-93.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6359416" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Organic ; Enzymes/physiology ; Kinetics ; Metabolism ; Nucleic Acid Conformation ; Nucleic Acids/physiology ; Organic Chemistry Phenomena ; Protein Conformation ; Solvents ; Water/*physiology
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  • 17
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    Genes of the major histocompatibility complex in mouse and man (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-11-18
    Description: The genes of the major histocompatibility complex code for cell-surface molecules that play an important role in the generation of the immune response. These genes and molecules have been studied intensively over the last five decades by geneticists, biochemists, and immunologists, but only recently has the isolation of the genes by molecular biologists facilitated their precise characterization. Many surprising findings have been made concerning their structure, multiplicity, organization, function, and evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steinmetz, M -- Hood, L -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):727-33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356354" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Chromosome Mapping ; Genes ; H-2 Antigens/*genetics ; HLA Antigens/*genetics ; Histocompatibility Antigens/genetics ; Humans ; *Major Histocompatibility Complex ; Mice ; Polymorphism, Genetic ; Protein Conformation
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    Fourier transform infrared difference spectra of intermediates in rhodopsin bleaching (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-03-18
    Description: The membrane protein rhodopsin is the primary light receptor in vision. Fourier transform infrared difference spectroscopy is sensitive to conformational changes in both the protein and the retinylidene chromophore of rhodopsin. By blocking rhodopsin bleaching at specific intermediates, it is possible to elucidate some of the primary molecular events of vision.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rothschild, K J -- Cantore, W A -- Marrero, H -- New York, N.Y. -- Science. 1983 Mar 18;219(4590):1333-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6828860" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Fourier Analysis ; Protein Conformation ; *Retinal Pigments ; *Rhodopsin ; Spectrophotometry, Infrared ; *Vision, Ocular
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    DNA-binding proteins (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-09-09
    Description: The structures of three proteins that regulate gene expression have been determined recently and suggest how these proteins may bind to their specific recognition sites on the DNA. One protein (Cro) is a repressor of gene expression, the second (CAP) usually stimulates gene expression, and the third (lambda repressor) can act as either a repressor or an activator. The three proteins contain a substructure consisting of two consecutive alpha helices that is virtually identical in each case. Structural and amino acid sequence comparisons suggest that this bihelical fold occurs in a number of proteins that regulate gene expression, and is an intrinsic part of the DNA-protein recognition event. The modes of repression and activation by Cro and lambda repressor are understood reasonably well, but the mode of action of CAP is still unclear.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takeda, Y -- Ohlendorf, D H -- Anderson, W F -- Matthews, B W -- GM20066/GM/NIGMS NIH HHS/ -- GM28138/GM/NIGMS NIH HHS/ -- GM30894/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Sep 9;221(4615):1020-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6308768" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; *DNA Helicases ; DNA-Binding Proteins ; Escherichia coli/genetics ; Gene Expression Regulation ; Models, Chemical ; Protein Conformation
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    Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-14
    Description: The amino acid sequences of mouse brain Thy-1 glycoproteins are shown to be homologous to those of variable-region immunoglobulin domains. There is also good homology with constant domains and beta 2-microglobulin; overall the results suggest that Thy-1 may be like the primordial immunoglobulin domain. Preliminary evidence for an invertebrate Thy-1 homolog supports this possibility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, A F -- Gagnon, J -- New York, N.Y. -- Science. 1982 May 14;216(4547):696-703.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6177036" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*immunology ; Antigens, Thy-1 ; Biological Evolution ; Epitopes ; Glycoproteins/*immunology ; Immunoglobulin Constant Regions/immunology ; Immunoglobulin Variable Region/immunology ; Immunoglobulins/*immunology ; Isoantibodies/biosynthesis ; Protein Conformation
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    Nucleotide sequence of the p21 transforming protein of Harvey murine sarcoma virus (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-09-03
    Description: Harvey murine sarcoma virus is a retrovirus which transforms cells by means of a single virally encoded protein called p21 has. We have determined the nucleotide sequence of 1.0 kilobase in the 5' half of the viral genome which encompasses the has coding sequences and its associated regulatory signals. The nucleotide sequence has identified the amino acid sequence of two additional overlapping polypeptides which share their reading frames and the carboxyl termini with p21 but which contain additional NH2-terminal amino acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dhar, R -- Ellis, R W -- Shih, T Y -- Oroszlan, S -- Shapiro, B -- Maizel, J -- Lowy, D -- Scolnick, E -- New York, N.Y. -- Science. 1982 Sep 3;217(4563):934-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6287572" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Transformation, Viral ; Cells, Cultured ; Defective Viruses/*genetics ; Genes, Viral ; Oncogene Protein p21(ras) ; Peptide Fragments ; Protein Biosynthesis ; Protein Conformation ; RNA, Viral/genetics ; Sarcoma Viruses, Murine/*genetics ; Viral Proteins/analysis/*genetics
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    Crystallization of the tetramer of histones H3 and H4 (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-05-28
    Description: Crystals of the histone tetramer (H3-H4)2 from calf thymus have been grown. The crystals yield x-ray diffraction patterns with Bragg spacings as small as 3.5 angstroms. Crystals grown from two types of preparations have the symmetry of the space group P61 (or P65). The best crystals were grown from histones that had the amino terminal arms removed by mild trypsinization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lattman, E -- Burlingame, R -- Hatch, C -- Moudrianakis, E N -- New York, N.Y. -- Science. 1982 May 28;216(4549):1016-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7079748" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; *Histones ; Nucleosomes/ultrastructure ; Protein Binding ; Protein Conformation
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    Penicillin target enzyme and the antibiotic binding site (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-10-29
    Description: The three-dimensional structure of a penicillin-sensitive D-alanyl-carboxypeptidase-transpeptidase has been determined by x-ray crystallography to a resolution of 2.8 angstroms. The site of binding of the beta-lactam antibiotics penicillin and cephalosporin has been located. These findings constitute direct observation of the interaction of beta-lactams with a transpeptidase enzyme and establish the feasibility of defining the molecular stereochemistry of this interaction for purposes of drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelly, J A -- Moews, P C -- Knox, J R -- Frere, J M -- Ghuysen, J M -- AI-13364-05/AI/NIAID NIH HHS/ -- AI-16702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1982 Oct 29;218(4571):479-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123246" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; *Carboxypeptidases ; *Cephalosporins ; Crystallography ; Models, Molecular ; *Muramoylpentapeptide Carboxypeptidase ; *Penicillins ; Protein Conformation ; X-Ray Diffraction
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  • 24
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    Infrared spectrum of the purple membrane: clue to a proton conduction mechanism? (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-04-23
    Description: The infrared spectrum of the purple membrane of Halobacterium halobium has amide I and amide A frequencies that are anomalously high for standard alpha-helical structures. Normal mode calculations indicate that these and other unusual features of the spectrum can be attributed to alpha 11-helices. Such structures suggest that the helix backbone may provide the framework through which proton transport takes place.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krimm, S -- Dwivedi, A M -- New York, N.Y. -- Science. 1982 Apr 23;216(4544):407-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6280277" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacteriorhodopsins ; Biological Transport, Active ; *Carotenoids ; Halobacterium/*ultrastructure ; Hydrogen Bonding ; Ion Channels ; Protein Conformation ; Protons ; Spectrophotometry, Infrared
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    Rational approaches to chemotherapy: antisickling agents (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klotz, I M -- Haney, D N -- King, L C -- New York, N.Y. -- Science. 1981 Aug 14;213(4509):724-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256275" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*drug therapy ; Aspirin/analogs & derivatives/therapeutic use ; Chemical Phenomena ; Chemistry ; *Hemoglobin, Sickle ; Humans ; Protein Binding/drug effects ; Protein Conformation ; Salicylates/*therapeutic use ; Solubility ; Structure-Activity Relationship
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    Diameter of the cell-to-cell junctional membrane channels as probed with neutral molecules (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-07-31
    Description: The cell-to-cell channels in the junctions of an insect salivary gland and of insect and mammalian cells in culture were probed with fluorescent molecules-neutral linear oligosaccharides, neutral branched glycopeptides, and charged linear peptides. From the molecular dimensions of the largest permeants and smallest impermeants the permeation-limiting channel diameter was obtained: 16 to 20 angstroms for the mammalian cells and 20 to 30 angstroms for the insect cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwarzmann, G -- Wiegandt, H -- Rose, B -- Zimmerman, A -- Ben-Haim, D -- Loewenstein, W R -- CA 14464/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 31;213(4507):551-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7244653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chironomidae ; Fluorescent Dyes ; Glycopeptides/*metabolism ; Intercellular Junctions/*ultrastructure ; Mice ; Mice, Inbred BALB C ; Models, Molecular ; Oligosaccharides/*metabolism ; Protein Conformation ; Salivary Glands/*ultrastructure ; Species Specificity
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    Cross-linked fibrinogen dimers demonstrate a feature of the molecular packing in fibrin fibers (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-01-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fowler, W E -- Erickson, H P -- Hantgan, R R -- McDonagh, J -- Hermans, J -- HL 20319/HL/NHLBI NIH HHS/ -- HL 23454/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1981 Jan 16;211(4479):287-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6108612" target="_blank"〉PubMed〈/a〉
    Keywords: Factor XIII/metabolism ; *Fibrin/metabolism ; *Fibrinogen/metabolism ; Humans ; Macromolecular Substances ; Microscopy, Electron ; Protein Conformation ; gamma-Glutamyltransferase/metabolism
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    A new understanding of sickle cell emerges (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-01-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maugh, T H 2nd -- New York, N.Y. -- Science. 1981 Jan 16;211(4479):265-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444466" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*blood ; Erythrocytes, Abnormal/pathology ; *Hemoglobin, Sickle ; Humans ; Protein Binding ; Protein Conformation ; Temperature
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    Real-time color graphics in studies of molecular interactions (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-02-13
    Description: Studies of the structures and interactions of large biological molecules require both coordinate data and three-dimensional visualization. Orthodox molecular models often bear a tenuous relationship to the coordinate data. In contrast, computer graphics requires that the display directly and accurately represent the data, and storage of modified configurations and recovery of original structures are simple. Software has been developed that allows real-time display of color line and surface displays of several interacting molecules, while quantitatively monitoring the stereochemistry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Langridge, R -- Ferrin, T E -- Kuntz, I D -- Connolly, M L -- GM 19267/GM/NIGMS NIH HHS/ -- RR-1081-03/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 Feb 13;211(4483):661-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7455704" target="_blank"〉PubMed〈/a〉
    Keywords: Carboxypeptidases/antagonists & inhibitors ; Color ; *Computers ; Macromolecular Substances ; *Models, Molecular ; *Models, Structural ; Nucleic Acid Conformation ; Protein Conformation ; Trypsin ; Trypsin Inhibitors ; Water
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    Structural changes at the heme induced by freezing hemoglobin (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-08-07
    Description: A dramatic change occurs in the vibrational properties of the iron-histidine bond, trans to the oxygen binding site, on freezing deoxyhemoglobin. The large, quaternary structure-dependent differences in the shape and frequency of the iron-histidine mode observed in resonance Raman scattering measurements above freezing ae significantly diminished by the freezing event and the scattering intensity increases substantially. On further reduction in temperature to 10 K this broad line becomes narrow and shifts to a higher frequency. These data implicate dynamical processes and protein interaction with water as contributors to the quaternary structure dependence of the iron-histidine bond and thus reflect on the role of that bond in the energetics of cooperative ligand binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ondrias, M R -- Rousseau, D L -- Simon, S R -- New York, N.Y. -- Science. 1981 Aug 7;213(4508):657-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256263" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; *Freezing ; *Heme ; *Hemoglobin A ; Histidine ; Humans ; Motion ; Protein Conformation ; Spectrum Analysis, Raman ; Water
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    Cadmium-113 nuclear magnetic resonance studies of bovine insulin: two-zinc insulin hexamer specifically binds calcium (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-05-01
    Description: By use of cadmium-113 nuclear magnetic resonance spectroscopy, a specific calcium ion binding site has been identified in the bovine two-zinc insulin hexamer. This site is composed of six glutamyl carboxylate groups clustered in the center of the hexamer, and is distinct from the normal zinc ion binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudmeier, J L -- Bell, S J -- Storm, M C -- Dunn, M F -- 5S05RR 07010-09/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 May 1;212(4494):560-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010607" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cadmium ; Calcium/*metabolism ; Cattle ; *Insulin/metabolism ; Isotopes ; Ligands ; Macromolecular Substances ; Magnetic Resonance Spectroscopy ; Protein Conformation ; Zinc/*metabolism
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    Bioactive conformation of luteinizing hormone-releasing hormone: evidence from a conformationally constrained analog (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-11-07
    Description: An analog of luteinizing hormone-releasing hormone containing a gamma-lactam as a conformational constraint has been prepared with the use of a novel cyclization of a methionine sulfonium salt. The analog is more active as a luteinizing hormone-releasing hormone agonist that the parent hormone, and provides evidence for a bioactive conformation containing a beta-turn.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freidinger, R M -- Veber, D F -- Perlow, D S -- Brooks, J R -- Saperstein, R -- New York, N.Y. -- Science. 1980 Nov 7;210(4470):656-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001627" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Assay ; Cells, Cultured ; Female ; *Gonadotropin-Releasing Hormone/analogs & derivatives ; Hydrogen Bonding ; Lactams ; Protein Conformation ; Rats ; Structure-Activity Relationship
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    Collagen: molecular diversity in the body's protein scaffold (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-03-21
    Description: Intensive research in the last decade has revealed a wealth of detail on the mechanism of biosynthesis, molecular structure, and covalent cross-linking of collagen. Tissues of higher animals express a family of at least five genetically distinct types of collagen molecule, each apparently tailored for different construction work outside the cell. Within each genetic type of collagen, further chemical heterogeneity is also evident; the variations in hydroxylation, glycosylation, and cross-linking are dependent, for example, on tissue type, age, and hormonal status. The functional significance of collagen's molecular diversity and its control by different cells and tissues are not yet well understood but abnormalities of collagen in many human diseases keep this protein a focal molecule of medical research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eyre, D R -- New York, N.Y. -- Science. 1980 Mar 21;207(4437):1315-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7355290" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcification, Physiologic ; Cartilage/ultrastructure ; *Collagen/genetics/metabolism ; Epithelium/ultrastructure ; Extracellular Space/ultrastructure ; Humans ; Hydrogen Bonding ; Polymorphism, Genetic ; Protein Biosynthesis ; Protein Conformation ; Vertebrates
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    Modeling coordination sites in metallobiomolecules (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-07-11
    Description: Synthetic metal complexes can closely approach the properties of metal ions in proteins and yield useful information concerning biological structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ibers, J A -- Holm, R H -- New York, N.Y. -- Science. 1980 Jul 11;209(4453):223-35.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384796" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Electron Transport ; Humans ; Iron-Sulfur Proteins ; *Metalloproteins ; *Metals ; Molecular Conformation ; Myoglobin ; Oxygen/blood ; Oxyhemoglobins ; Protein Binding ; Protein Conformation
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    Hormone binding alters the conformation of the insulin receptor (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-12-05
    Description: Fat cells or fat cell membranes were briefly subjected to mild proteolysis under conditions where insulin receptors were either free or bound to (125)I-labeled insulin. When receptors were then affinity-labeled to visualize the effects of this treatment, it was observed that receptors that had been occupied by ligand during proteolysis exhibited greater rates of degradation than unoccupied receptors. These results demonstrate that insulin-receptor interaction induces a change in receptor structure that may be related to signal transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pilch, P F -- Czech, M P -- AM 06069/AM/NIADDK NIH HHS/ -- AM 17893/AM/NIADDK NIH HHS/ -- HD 11343/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1980 Dec 5;210(4474):1152-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7003712" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Cell Membrane/metabolism ; Insulin/*metabolism ; Male ; Peptide Fragments/analysis ; Protein Binding ; Protein Conformation ; Rats ; Receptor, Insulin/*metabolism ; Trypsin/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Assembly of proteins into membranes (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-11-21
    Description: Two pathways for protein assembly into biological membranes have been proposed. The "signal hypothesis" emphasizes the role of specific membrane proteins in binding the growing polypeptide and conducting it into the bilayer during its synthesis. The "membrane-triggered folding" hypothesis emphasizes self-assembly and the role of changing protein conformation during transfer from an aqueous compartment into a membrane. These ideas provide a framework for reviewing recent data on the biogenesis of membrane proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickner, W -- New York, N.Y. -- Science. 1980 Nov 21;210(4472):861-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001628" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Membrane Proteins/*metabolism ; Membranes/enzymology/*metabolism ; Protein Conformation ; Protein Precursors/metabolism ; Proteins/secretion ; Solubility ; Viral Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Folic acid: crystal structure and implications for enzyme binding (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-17
    Description: The crystal and molecular structure of folic acid dihydrate has been determined by x-ray diffraction. Folic acid is in an extended conformation with the pteridine ring in the keto form. The C(4) oxygen and N(10) atoms are on the same side of the molecule, hydrogen-bonded to the same water. This conformation has the pteridine rotated approximately 180 degrees away from the orientation of the pteridine ring of methotrexate bound to dihydrofolate reductase. The folic acid pteridine and phenyl rings interact in a stacking manner which is suggestive of the type of associations these groups could form in a complex of folate, dihydrofolate reductase, and reduced nicotinamide adenine dinucleotide phosphate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mastropaolo, D -- Camerman, A -- Camerman, N -- CA-15879/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct 17;210(4467):334-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7423195" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography ; *Folic Acid ; Molecular Conformation ; Protein Conformation ; Tetrahydrofolate Dehydrogenase ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Catecholamine-induced alteration in sedimentation behavior of membrane bound beta-adrenergic receptors (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-01
    Description: Incubation of astrocytoma cells with catecholamines results in a decrease in catecholamine-stimulated adenylate cyclase activity and a concomitant alteration in the sedimentation properties of particulate beta-adrenergic receptors. The altered receptors exhibit agonist binding properties similar to those of receptors that are "uncoupled" from adenylate cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harden, T K -- Cotton, C U -- Waldo, G L -- Lutton, J K -- Perkins, J P -- GM 25163/GM/NIGMS NIH HHS/ -- HL 22490/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct;210(4468):441-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6254143" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Astrocytoma ; Cell Line ; Centrifugation, Density Gradient ; Concanavalin A/pharmacology ; Endocytosis ; Humans ; Isoproterenol/*metabolism ; Protein Conformation ; Receptors, Adrenergic/*metabolism ; Receptors, Adrenergic, beta/*metabolism ; Time Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 39
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    Monte Carlo simulation of water behavior around the dipeptide N-acetylalanyl-N-methylamide (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-09
    Description: Applications of Monte Carlo and molecular dynamics computer simulation techniques indicate that they are potentially powerful tools for understanding biological systems at the molecular level. The Monte Carlo technique can be used to study the solvent structure around a small peptide and the effect of the aqueous environment on the conformational equilibria of the peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagler, A T -- Osguthorpe, D J -- Robson, B -- New York, N.Y. -- Science. 1980 May 9;208(4444):599-601.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7367882" target="_blank"〉PubMed〈/a〉
    Keywords: *Alanine/*analogs & derivatives ; *Dipeptides ; Models, Chemical ; Monte Carlo Method ; Protein Conformation ; Solvents ; *Water
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Acetylcholine receptor: complex of homologous subunits (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-06-27
    Description: The acetylcholine receptor from the electric ray Torpedo californica is composed of five subunits; two are identical and the other three are structurally related to them. Microsequence analysis of the four polypeptides demonstrates amino acid homology among the subunits. Further sequence analysis of both membrane-bound and Triton-solubilized, chromatographically purified receptor gave the stoichiometry of the four subunits (40,000:50,000:60,000:65,000 daltons) as 2:1:1:1, indicating that this protein is a pentameric complex with a molecular weight of 255,000 daltons. Genealogical analysis suggests that divergence from a common ancestral gene occurred early in the evolution of the receptor. This shared ancestry argues that each of the four subunits plays a functional role in the receptor's physiological action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raftery, M A -- Hunkapiller, M W -- Strader, C D -- Hood, L E -- New York, N.Y. -- Science. 1980 Jun 27;208(4451):1454-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384786" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Amino Acid Sequence ; Animals ; Electric Organ/*analysis ; Fishes ; Macromolecular Substances ; Molecular Weight ; Protein Conformation ; *Receptors, Cholinergic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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