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  • Artikel  (5)
  • Neueste Artikel (Zeitschrifteninhaltsverzeichnisse / in press)  (5)
  • Protein Conformation
  • American Association for the Advancement of Science (AAAS)  (5)
  • Annual Reviews
  • 2010-2014
  • 1980-1984  (5)
  • 1965-1969
  • 1955-1959
  • 1930-1934
  • 1982  (5)
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  • Artikel  (5)
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  • Neueste Artikel (Zeitschrifteninhaltsverzeichnisse / in press)  (5)
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  • American Association for the Advancement of Science (AAAS)  (5)
  • Annual Reviews
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  • 2010-2014
  • 1980-1984  (5)
  • 1965-1969
  • 1955-1959
  • 1930-1934
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  • 1
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    Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1982-05-14
    Beschreibung: 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〉
    Schlagwort(e): 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
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
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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
    Publikationsdatum: 1982-09-03
    Beschreibung: 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〉
    Schlagwort(e): 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
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
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    Crystallization of the tetramer of histones H3 and H4 (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1982-05-28
    Beschreibung: 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〉
    Schlagwort(e): Crystallization ; *Histones ; Nucleosomes/ultrastructure ; Protein Binding ; Protein Conformation
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
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    Penicillin target enzyme and the antibiotic binding site (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1982-10-29
    Beschreibung: 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〉
    Schlagwort(e): Binding Sites ; *Carboxypeptidases ; *Cephalosporins ; Crystallography ; Models, Molecular ; *Muramoylpentapeptide Carboxypeptidase ; *Penicillins ; Protein Conformation ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
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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)
    Details
    Publikationsdatum: 1982-04-23
    Beschreibung: 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〉
    Schlagwort(e): *Bacteriorhodopsins ; Biological Transport, Active ; *Carotenoids ; Halobacterium/*ultrastructure ; Hydrogen Bonding ; Ion Channels ; Protein Conformation ; Protons ; Spectrophotometry, Infrared
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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