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  • Protein Conformation
  • American Association for the Advancement of Science (AAAS)  (19)
  • American Chemical Society
  • Cell Press
  • National Academy of Sciences
  • 1995-1999
  • 1985-1989  (19)
  • 1980-1984
  • 1975-1979
  • 1940-1944
  • 1985  (19)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (19)
  • American Chemical Society
  • Cell Press
  • National Academy of Sciences
Years
  • 1995-1999
  • 1985-1989  (19)
  • 1980-1984
  • 1975-1979
  • 1940-1944
Year
  • 1
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    Intrinsic and extrinsic factors in protein antigenic structure (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-06
    Description: Recent advances in the preparation of synthetic peptide vaccines and the use of synthetic peptides as probes of antigenic structure and function have led to renewed interest in the prediction of antigenic sites recognized by antibodies and T cells. This review focuses on antibodies. Features intrinsic to the antigen, such as hydrophilicity and mobility, may be useful in the selection of amino acid sequences of the native protein that will elicit antibodies cross-reacting with peptides, or sequences which, as peptides, will be more likely to elicit antibodies cross-reactive with the native protein. Structural mobility may also contribute to protein-protein interactions in general. However, the entire accessible surface of a protein is likely to be detectable by a large enough panel of antibodies. Which of these antibodies are made in any individual depends on factors extrinsic to the antigen molecule, host factors such as self-tolerance, immune response genes, idiotype networks, and the immunoglobulin structural gene repertoire.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berzofsky, J A -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):932-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2410982" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibody Specificity ; Antigen-Antibody Complex ; B-Lymphocytes/immunology ; Clone Cells/immunology ; *Epitopes ; Genes ; Genes, MHC Class II ; Humans ; Immune Tolerance ; Immunoglobulin Idiotypes ; Lymphocyte Cooperation ; Motion ; Myoglobin/immunology ; Probability ; Protein Conformation ; Proteins/*immunology ; Solubility ; Structure-Activity Relationship ; Surface Properties ; T-Lymphocytes, Helper-Inducer/immunology ; T-Lymphocytes, Regulatory/immunology ; Water
    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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    In vivo function and membrane binding properties are correlated for Escherichia coli lamB signal peptides (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-31
    Description: Wild-type and pseudorevertant signal peptides of the lamB gene product of Escherichia coli interact with lipid systems whereas a nonfunctional deletion mutant signal peptide does not. This conclusion is based on interaction of synthetic signal peptides with a lipid monolayer-water surface, conformational changes induced by presence of lipid vesicles in an aqueous solution of signal peptide, and capacities of the peptides to promote vesicle aggregation. Analysis of the signal sequences and previous conformational studies suggest that these lipid interaction properties may be attributable to the tendency of the functional signal peptides to adopt alpha-helical conformations. Although the possibility of direct interaction between the signal peptide and membrane lipids during protein secretion is controversial, the results suggest that conformationally related amphiphilicity and consequent membrane affinity of signal sequences are important for function in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Briggs, M S -- Gierasch, L M -- Zlotnick, A -- Lear, J D -- DeGrado, W F -- AM-27616/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1985 May 31;228(4703):1096-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3158076" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/*metabolism ; Bacteriophage lambda/metabolism ; Biological Transport ; Chemistry, Physical ; Circular Dichroism ; Membrane Lipids/metabolism ; Models, Biological ; Peptides/*metabolism ; Phospholipids/*metabolism ; Physicochemical Phenomena ; Porins ; Protein Conformation ; Protein Sorting Signals ; Receptors, Virus/*metabolism ; Structure-Activity Relationship ; Surface Properties ; Water
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  • 3
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    Crystallographic structure of the octameric histone core of the nucleosome at a resolution of 3.3 A (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-03
    Description: The structure of the (H2A-H2B-H3-H4)2 histone octamer has been determined by means of x-ray crystallographic techniques at a resolution of 3.3 angstroms. The octamer is a prolate ellipsoid 110 angstroms long and 65 to 70 angstroms in diameter, and its general shape is that of a rugby ball. The size and shape are radically different from those determined in earlier studies. The most striking feature of the histone octamer is its tripartite organization, that is, a central (H3-H4)2 tetramer flanked by two H2A-H2B dimers. The DNA helix, placed around the octamer in a path suggested by the features on the surface of the protein, appears like a spring holding the H2A-H2B dimers at either end of the (H3-H4)2 tetramer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burlingame, R W -- Love, W E -- Wang, B C -- Hamlin, R -- Nguyen, H X -- Moudrianakis, E N -- New York, N.Y. -- Science. 1985 May 3;228(4699):546-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3983639" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chickens ; Chromatin/ultrastructure ; DNA/metabolism ; *Histones/metabolism ; Models, Chemical ; Nucleosomes/*ultrastructure ; Protein Conformation ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 4
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    Molecular structure of troponin C from chicken skeletal muscle at 3-angstrom resolution (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-22
    Description: The x-ray structure of chicken skeletal muscle troponin C (TnC), the Ca2+-binding subunit of the troponin complex, shows that the protein is about 70 angstroms long with an unusual dumbbell shape. The carboxyl and amino domains are separated by a single long alpha helix of about nine turns. Only the two high-affinity Ca2+-Mg2+ sites of the COOH-domain are occupied by metal ions resulting in conformational differences between the COOH- and NH2-domains. These differences are probably important in the triggering of muscle contraction by TnC. Also the structure of TnC is relevant in understanding the function of other calcium-regulated proteins, in particular that of calmodulin because of its strong similarity in amino acid sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sundaralingam, M -- Bergstrom, R -- Strasburg, G -- Rao, S T -- Roychowdhury, P -- Greaser, M -- Wang, B C -- AM-34139/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1985 Feb 22;227(4689):945-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3969570" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calmodulin/physiology ; Chickens ; Muscle Contraction ; Muscles/physiology/ultrastructure ; Protein Conformation ; Troponin/*physiology ; Troponin C ; Turkeys ; X-Ray Diffraction
    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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  • 5
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    A model for fibrinogen: domains and sequence (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-20
    Description: Electron microscopy of rotary-shadowed fibrinogen demonstrates that the molecules modified for crystallization by limited cleavage with a bacterial protease retain the major features of the native structure. This evidence, together with image processing and x-ray analysis of the crystals and of fibrin, has been used to develop a three-dimensional low resolution model for the molecule. The data indicate that the two large end domains of the molecule would be composed of the carboxyl-terminus of the B beta chain (proximal) and gamma chain (distal), respectively; the carboxyl-terminus of the A alpha chain would fold back to form an additional central domain. On this basis, the carboxyl-terminal region of each of the three chains of fibrinogen is folded independently into a globular domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weisel, J W -- Stauffacher, C V -- Bullitt, E -- Cohen, C -- AM17346/AM/NIADDK NIH HHS/ -- GM07596-07/GM/NIGMS NIH HHS/ -- HL30954/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1388-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071058" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Computers ; Fibrinogen/*metabolism ; Microscopy, Electron ; Models, Molecular ; Protein Conformation
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  • 6
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    Picosecond time-resolved resonance Raman studies of hemoglobin: implications for reactivity (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-16
    Description: Picosecond time-resolved Raman spectra of hemoglobin generated with blue pulses (20 to 30 picoseconds) that were resonant with the Soret band and of sufficient intensity to completely photodissociate the starting liganded sample are reported. For both R- and T-state liganded hemoglobins, the peak frequencies in the spectrum of the deoxy transient were the same at approximately 25 picoseconds as those observed at 10 nanoseconds subsequent to photodissociation. In particular, the large R-T differences in the frequency of the stretching mode for the iron-proximal histidine bond (VFe-His) detected in previously reported nanosecond-resolved spectra were also evident in the picosecond-resolved spectra. The implications of this finding with respect to the distribution of strain energy in the liganded protein and the origin of the time course for geminate recombination are discussed. On the basis of these results, a microscopic model is proposed in which delocalization of strain energy is strongly coupled to the coordinate of the iron. The model is used to explain the origin of the R-T differences in the rates of ligand dissociation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Findsen, E W -- Friedman, J M -- Ondrias, M R -- Simon, S R -- 2-506 RR-8139/RR/NCRR NIH HHS/ -- R01 GM3333O-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 16;229(4714):661-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023704" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; *Hemoglobin A ; Humans ; Motion ; Protein Conformation ; Spectrum Analysis, Raman ; Structure-Activity Relationship ; Thermodynamics
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  • 7
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    Three-dimensional structure of poliovirus at 2.9 A resolution (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-27
    Description: The three-dimensional structure of poliovirus has been determined at 2.9 A resolution by x-ray crystallographic methods. Each of the three major capsid proteins (VP1, VP2, and VP3) contains a "core" consisting of an eight-stranded antiparallel beta barrel with two flanking helices. The arrangement of beta strands and helices is structurally similar and topologically identical to the folding pattern of the capsid proteins of several icosahedral plant viruses. In each of the major capsid proteins, the "connecting loops" and NH2- and COOH-terminal extensions are structurally dissimilar. The packing of the subunit "cores" to form the virion shell is reminiscent of the packing in the T = 3 plant viruses, but is significantly different in detail. Differences in the orientations of the subunits cause dissimilar contacts at protein-protein interfaces, and are also responsible for two major surface features of the poliovirion: prominent peaks at the fivefold and threefold axes of the particle. The positions and interactions of the NH2- and COOH-terminal strands of the capsid proteins have important implications for virion assembly. Several of the "connecting loops" and COOH-terminal strands form prominent radial projections which are the antigenic sites of the virion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hogle, J M -- Chow, M -- Filman, D J -- AI-20566/AI/NIAID NIH HHS/ -- AI-22346/AI/NIAID NIH HHS/ -- NS-07078/NS/NINDS NIH HHS/ -- R01 AI020566/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Sep 27;229(4720):1358-65.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/immunology ; Capsid/physiology ; Chemical Phenomena ; Chemistry ; HeLa Cells/microbiology ; Mutation ; Poliovirus/physiology/*ultrastructure ; Protein Conformation ; Virus Replication ; X-Ray Diffraction
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  • 8
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    Systematic variation in DNA length yields highly ordered repressor-operator cocrystals (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-20
    Description: Crystals have been grown that contain the operator-binding domain of the lambda repressor and the lambda operator site OL1. Crystallization conditions were tested with a set of DNA fragments, ranging in length from 17 to 23 base pairs. The best crystals were grown with a 20-base pair DNA fragment. These crystals have space-group symmetry P2I, with unit cell dimensions a = 37.1 A, b = 68.8 A, c = 56.8 A, and a beta angle of 91.5 degrees. They diffracted to at least 2.5 A resolution. High resolution data from these crystals should allow the direct determination of how a repressor recognizes its operator site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jordan, S R -- Whitcombe, T V -- Berg, J M -- Pabo, C O -- GM 31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1383-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3906896" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromatography, High Pressure Liquid ; Crystallization ; DNA, Bacterial/*genetics ; Escherichia coli/genetics ; *Gene Expression Regulation ; Nucleic Acid Conformation ; Protein Conformation ; Repressor Proteins/*genetics/isolation & purification ; Structure-Activity Relationship ; Transcription Factors/*genetics ; X-Ray Diffraction
    Print ISSN: 0036-8075
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  • 9
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    Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-04
    Description: A 2.7 angstrom resolution x-ray diffraction analysis of a trypsin-modified form of the Escherichia coli elongation factor Tu reveals that the GDP-binding domain has a structure similar to that of other nucleotide-binding proteins. The GDP ligand is located at the COOH-terminal end of the beta sheet and is linked to the protein via a Mg2+ ion salt bridge. The location of the guanine ring is unusual; the purine ring is located on the outer edge of the domain, not deep within a hydrophobic pocket. The amino acids from Pro10 to Arg44 and from Gly59 to Glu190 have been assigned to the electron density with computer graphic techniques, and the resulting model is consistent with all known biochemical data. An analysis of the structure reveals that four regions of the amino acid sequence that are homologous with the family of ras oncogene proteins, termed p21, are located in the vicinity of the GDP-binding site, and most of the invariant amino acids shared by the proteins interact directly with the GDP ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jurnak, F -- GM 26895/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):32-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3898365" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/*analysis ; Binding Sites ; Chemistry, Physical ; Computers ; Escherichia coli ; Fourier Analysis ; Guanine Nucleotides/*analysis ; Guanosine Diphosphate/*analysis ; Magnesium/metabolism ; *Oncogenes ; Peptide Elongation Factor Tu ; Peptide Elongation Factors/*analysis ; Physicochemical Phenomena ; Protein Conformation ; Trypsin/metabolism ; X-Ray Diffraction
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  • 10
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    A model for the tertiary structure of p21, the product of the ras oncogene (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-04
    Description: A model was developed for the structure of p21, the protein with a molecular weight of 21,000 that is produced by the ras genes. This model predicts that p21 consists of a central core of beta-sheet structure, connected by loops and alpha helices. Four of these loops comprise the guanine nucleotide binding site. The phosphoryl binding region is made up of amino acid sequences from 10 to 16 and from 57 to 63 of p21. The latter sequence may contain a site for magnesium binding. Amino acids defining guanine specificity are Asn-116 and Asp-119, and sequences around amino acid 145 may contribute to guanine binding. The model makes it possible to visualize how oncogenic mutations of p21 affect interaction with guanine nucleotides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCormick, F -- Clark, B F -- la Cour, T F -- Kjeldgaard, M -- Norskov-Lauritsen, L -- Nyborg, J -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):78-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3898366" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/analysis ; Animals ; *Aspartate Carbamoyltransferase ; Base Sequence ; Binding Sites ; *Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) ; Cattle ; *Dihydroorotase ; Escherichia coli ; Guanine Nucleotides/metabolism ; Humans ; Macromolecular Substances ; Magnesium/metabolism ; Membrane Proteins/analysis ; Models, Chemical ; *Multienzyme Complexes ; Mutation ; *Oncogenes ; Peptide Elongation Factor Tu ; Peptide Elongation Factors/analysis ; Protein Conformation ; Proteins/*analysis ; RNA, Transfer, Amino Acyl/metabolism ; Saccharomyces cerevisiae ; Transducin
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  • 11
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    Localized control of ligand binding in hemoglobin: effect of tertiary structure on picosecond geminate recombination (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-12
    Description: The picosecond geminate rebinding of molecular oxygen was monitored in a variety of different human, reptilian, and fish hemoglobins. The fast (100 to 200 picoseconds) component of the rebinding is highly sensitive to protein structure. Both proximal and distal perturbations of the heme affect this rebinding process. The rebinding yield for the fast process correlates with the frequency of the stretching motion of the iron-proximal histidine mode (VFe-His) observed in the transient Raman spectra of photodissociated ligated hemoglobins. The high-affinity R-state species exhibit the highest values for VFe-His and the highest yields for fast rebinding, whereas low affinity R-state species and T-state species exhibit lower values of VFe-His and correspondingly reduced yields for this geminate process. These findings link protein control of ligand binding with events at the heme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Friedman, J M -- Scott, T W -- Fisanick, G J -- Simon, S R -- Findsen, E W -- Ondrias, M R -- Macdonald, V W -- 1 R01 GM 33330-1/GM/NIGMS NIH HHS/ -- DHHS2-S06/DH/BHP HRSA HHS/ -- RR08139/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1985 Jul 12;229(4709):187-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4012316" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Fishes ; Heme/metabolism ; Hemoglobins, Abnormal/*genetics/metabolism ; Humans ; Ligands/metabolism ; Oxygen/metabolism ; Protein Binding ; Protein Conformation
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  • 12
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    Model structure for the inflammatory protein C5a (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-31
    Description: The complement cleavage product C5a is a potent stimulant of inflammatory processes; thus, inhibition of C5a activity is of therapeutic interest. The three-dimensional structure of the major portion of C5a was modeled from the homologous C3a crystal structure by comparative modeling techniques. The model shows that core residues of C5a are completely conserved, while external residues differ from C3a. Even though the amino-terminal 12 residues of C3a are disordered in the crystal, this sequence in C5a may form an amphipathic helix. The distribution of species sequence differences in the complete C5a structure suggests a possible receptor binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greer, J -- New York, N.Y. -- Science. 1985 May 31;228(4703):1055-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3992245" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Complement C5/metabolism ; Complement C5a ; Crystallography ; Humans ; Hydrogen Bonding ; Models, Molecular ; Protein Conformation ; Receptors, Complement/metabolism ; Thermodynamics
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  • 13
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    Dynamics and conformational energetics of a peptide hormone: vasopressin (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-03-15
    Description: A theoretical methodology for use in conjunction with experiment was applied to the neurohypophyseal hormone lysine vasopressin for elucidation of its accessible molecular conformations and associated flexibility, conformational transitions, and dynamics. Molecular dynamics and energy minimization techniques make possible a description of the conformational properties of a peptide in terms of the precise positions of atoms, their fluctuations in time, and the interatomic forces acting on them. Analysis of the dynamic trajectory of lysine vasopressin shows the ability of a flexible peptide hormone to undergo spontaneous conformational transitions. The excursions of an individual phenylalanine residue exemplify the dynamic flexibility and multiple conformational states available to small peptide hormones and their component residues, even within constraints imposed by a cyclic hexapeptide ring.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagler, A T -- Osguthorpe, D J -- Dauber-Osguthorpe, P -- Hempel, J C -- New York, N.Y. -- Science. 1985 Mar 15;227(4692):1309-15.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3975616" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Chemistry, Physical ; Energy Metabolism ; Hydrogen Bonding ; Lypressin/*metabolism ; Phenylalanine/metabolism ; Physicochemical Phenomena ; Protein Conformation
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  • 14
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    Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-19
    Description: The milk protein beta-lactoglobulin has been extensively studied but its function has not been identified. A clue regarding the function of a protein can be obtained by discovering a genetic relationship with a protein of known function through comparisons of amino acid sequence. Such comparisons revealed that beta-lactoglobulin is similar to human serum retinol-binding protein and to another human protein of unknown function known as complex-forming glycoprotein heterogeneous in charge (protein HC). beta-Lactoglobulins from several species have been found to bind retinol, while the absorption and fluorescence properties reported for the unidentified heterogeneous prosthetic group of protein HC are retinoid-like. The role of serum retinol-binding protein in vitamin A transport in the circulation suggests that the other two homologous proteins may function in the binding and transport of retinoids; beta-lactoglobulin may facilitate the absorption of vitamin A from milk and protein HC may mediate the excretion of retinol-derived metabolites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pervaiz, S -- Brew, K -- GM 21363/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):335-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2580349" target="_blank"〉PubMed〈/a〉
    Keywords: Alpha-Globulins/*genetics ; Amino Acid Sequence ; Animals ; Cattle ; Dolphins ; Humans ; Lactoglobulins/*genetics/metabolism ; Lagomorpha ; Mammals ; Milk/metabolism ; Primates ; Protein Conformation ; Proteinuria/metabolism ; Retinol-Binding Proteins/*genetics/metabolism ; Rodentia ; Swine ; Vitamin A/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 15
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    Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-23
    Description: The sequence of the entire RNA genome of the type flavivirus, yellow fever virus, has been obtained. Inspection of this sequence reveals a single long open reading frame of 10,233 nucleotides, which could encode a polypeptide of 3411 amino acids. The structural proteins are found within the amino-terminal 780 residues of this polyprotein; the remainder of the open reading frame consists of nonstructural viral polypeptides. This genome organization implies that mature viral proteins are produced by posttranslational cleavage of a polyprotein precursor and has implications for flavivirus RNA replication and for the evolutionary relation of this virus family to other RNA viruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rice, C M -- Lenches, E M -- Eddy, S R -- Shin, S J -- Sheets, R L -- Strauss, J H -- AI 10793/AI/NIAID NIH HHS/ -- AI 20612/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 23;229(4715):726-33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023707" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biological Evolution ; Gene Expression Regulation ; Genes ; Glycoproteins/genetics ; Nucleic Acid Conformation ; Protein Biosynthesis ; Protein Conformation ; Protein Processing, Post-Translational ; RNA, Viral/*genetics ; Viral Proteins/*genetics ; *Virus Replication ; Yellow fever virus/*genetics
    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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  • 16
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    The structure of a T = 1 icosahedral empty particle from southern bean mosaic virus (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-16
    Description: The structure of a T = 1 icosahedral particle (where T is the triangulation number), assembled from southern bean mosaic virus coat protein fragments that lacked the amino-terminal arm, was solved by means of model building procedures with the use of 6-angstrom resolution x-ray diffraction data. The icosahedral five-, three-, and twofold contacts were found to be similar, at this resolution, to the analogous contacts (icosahedral five-, quasi-three-, and quasi-twofolds) found in the parent T = 3 southern bean mosaic virus. However, the icosahedral fivefold contacts of the T = 3 structure are the most conserved in the T = 1 capsid. These results are consistent with a mechanism in which pentameric caps of dimers are the building blocks for the assembly of T = 1 and T = 3 icosahedral viruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erickson, J W -- Silva, A M -- Murthy, M R -- Fita, I -- Rossmann, M G -- New York, N.Y. -- Science. 1985 Aug 16;229(4714):625-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023701" target="_blank"〉PubMed〈/a〉
    Keywords: Capsid/ultrastructure ; Macromolecular Substances ; Models, Molecular ; Mosaic Viruses/*ultrastructure ; Protein Binding ; Protein Conformation ; *Viral Proteins ; X-Ray Diffraction
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    Structure, dynamics, and reactivity in hemoglobin (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-14
    Description: The static structure of hemoglobin and its functional properties are very well characterized. It is still not known how energy is stored and used within the structure of the protein to promote function and functional diversity. An essential part of this question is understanding the mechanism through which the overall protein structure (quaternary structure) couples to the local environment about the oxygen binding sites. Time-resolved resonance Raman spectroscopy has been used to probe the vibrational degrees of the freedom of the binding site as a function of protein structure. Comparison of the spectra from both equilibrium and transient forms of deoxy hemoglobin from a variety of mammalian, reptilian, and fish hemoglobins reveals that for each quaternary structure there exist two tertiary states stabilized by the presence or absence of an iron-bound ligand. Pulse-probe Raman experiments show that for photodissociated, ligated hemoglobins the local tertiary structure relaxes at a solution-dependent rate extending from tens of nanoseconds to microseconds. In this local environment, the linkage between the iron and the proximal histidine proves to be the single observed structural feature that responds in a systematic and substantial manner to structural changes in the protein. The additional finding of a correlation between the frequency of the iron-proximal histidine stretching motion (nu Fe-His) and various parameters of ligand reactivity, including geminate recombination, implicates the associated localized structural element in the mechanism of protein control of ligand binding. On the basis of these and related finds, a model is presented to account for both coarse and fine control of ligand binding by the protein structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Friedman, J M -- New York, N.Y. -- Science. 1985 Jun 14;228(4705):1273-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001941" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Animals ; Carboxyhemoglobin ; Cold Temperature ; *Hemoglobins ; Histidine ; Humans ; Hydrogen-Ion Concentration ; Iron ; *Oxyhemoglobins ; Protein Conformation ; Spectrum Analysis, Raman ; Structure-Activity Relationship ; Thermodynamics
    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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  • 18
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    Sequence and structure of a human glucose transporter (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-09-06
    Description: The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone. Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical. The protein lacks a cleavable amino-terminal signal sequence. Analysis of the primary structure suggests the presence of 12 membrane-spanning domains. Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves. The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face. Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mueckler, M -- Caruso, C -- Baldwin, S A -- Panico, M -- Blench, I -- Morris, H R -- Allard, W J -- Lienhard, G E -- Lodish, H F -- GM22996/GM/NIGMS NIH HHS/ -- HL32262/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):941-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3839598" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Carrier Proteins/genetics/metabolism ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/genetics ; Erythrocytes/metabolism ; Glucose/*metabolism ; Humans ; Liver Neoplasms, Experimental/metabolism ; *Membrane Proteins/genetics/metabolism ; Molecular Weight ; Monosaccharide Transport Proteins ; Protein Conformation ; RNA, Messenger/genetics ; Tissue Distribution
    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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  • 19
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    The structure of arthropod hemocyanins (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-09
    Description: Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. Comparison of the amino acid sequence data for seven different subunits of arthropod hemocyanins from crustaceans and chelicerates shows many highly conserved residues and extensive regions of near identity. This correspondence can be matched closely with the three domain structure established by x-ray crystallography for spiny lobster hemocyanin. The degree of identity is particularly striking in the second domain of the subunit that contains the six histidines which ligate the two oxygen-binding copper atoms. The polypeptide architecture of spiny lobster hemocyanin appears to be the same in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, about 540 to 600 million years ago.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linzen, B -- Soeter, N M -- Riggs, A F -- Schneider, H J -- Schartau, W -- Moore, M D -- Yokota, E -- Behrens, P Q -- Nakashima, H -- Takagi, T -- GM 21314/GM/NIGMS NIH HHS/ -- GM 28410/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 9;229(4713):519-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023698" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arachnida/genetics ; *Arthropods/genetics ; Binding Sites ; Biological Evolution ; Chemical Phenomena ; Chemistry ; Copper ; Crustacea/genetics ; *Hemocyanin/genetics ; Models, Molecular ; Protein Conformation ; Species Specificity
    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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