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  • Protein Conformation
  • American Association for the Advancement of Science (AAAS)  (5)
  • American Physical Society
  • Cell Press
  • 2020-2024
  • 2010-2014
  • 1980-1984  (5)
  • 1955-1959
  • 1980  (5)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (5)
  • American Physical Society
  • Cell Press
Years
  • 2020-2024
  • 2010-2014
  • 1980-1984  (5)
  • 1955-1959
Year
  • 1
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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)
    Details
    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
    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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  • 2
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    Collagen: molecular diversity in the body's protein scaffold (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 3
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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
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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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
    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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  • 5
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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
    Published by American Association for the Advancement of Science (AAAS)
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