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  • Artikel  (4)
  • Base Sequence
  • Binding Sites
  • American Association for the Advancement of Science (AAAS)  (4)
  • American Institute of Physics
  • 2020-2022
  • 1995-1999
  • 1980-1984  (4)
  • 1940-1944
  • 1982  (4)
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  • Artikel  (4)
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  • American Association for the Advancement of Science (AAAS)  (4)
  • American Institute of Physics
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  • 2020-2022
  • 1995-1999
  • 1980-1984  (4)
  • 1940-1944
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  • 1
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    Biospecific labeling with undecagold: visualization of the biotin-binding site on avidin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1982-10-15
    Beschreibung: The biotin-binding site on avidin has been labeled with biotin conjugated to undecagold, an organometallic cluster compound containing 11 gold atoms in a core angestroms in diameter. Examination of unstained specimens by scanning transmission electron microscopy reveals the labeled sites directly, without computational averaging or filtering of the images. This approach should be widely applicable for determining the locations of subunits and functional site in biological macromolecules at a resolution at a resolution in range of 15 angstroms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Safer, D -- Hainfeld, J -- Wall, J S -- Reardon, J E -- AM 28607/AM/NIADDK NIH HHS/ -- GM 12202/GM/NIGMS NIH HHS/ -- GM 28750/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Oct 15;218(4569):290-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123234" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Avidin/*metabolism ; Binding Sites ; Biotin/*metabolism ; Gold/*metabolism ; Organogold Compounds ; Organometallic Compounds/*metabolism ; Ovalbumin/*analogs & derivatives
    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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    DNA conformation, dynamics, and interactions in solution (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1982-05-07
    Beschreibung: The conformation and dynamics of the d(CGCGAATTCGCG) duplex, its analogs containing mismatched base pairs and helix interruptions, and its complexes with actinomycin and Netropsin, bound separately and simultaneously, have been investigated by nuclear magnetic resonance spectroscopy in aqueous solution. Structural information has been deduced from chemical shift and nuclear Overhauser effect parameters, while the kinetics have been probed from line width and saturation recovery experiments on proton and phosphorus markers at the individual base pair level. These studies lead to an improved understanding of the role of nucleic acid sequence on the structure, flexibility, and conformational interconversions in the duplex state. The nuclear magnetic resonance measurements readily identify helix modification and antibiotic binding sites on the nucleic acid and estimate the extent to which the observed conformational and dynamic perturbations are transmitted to adjacent base pair regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patel, D J -- Pardi, A -- Itakura, K -- New York, N.Y. -- Science. 1982 May 7;216(4546):581-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6280281" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Dna ; Dactinomycin ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Motion ; Netropsin ; *Nucleic Acid Conformation ; Oligodeoxyribonucleotides ; Protons ; Structure-Activity Relationship ; Temperature
    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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    Diverse mechanisms in the generation of human beta-tubulin pseudogenes (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1982-08-06
    Beschreibung: The sequence of two human beta-tubulin pseudogenes is described. One contains an intervening sequence but lacks sequences encoding the 55 N-terminal amino acids of the polypeptide chain. A second has no introns but has a polyadenylate signal and an oligoadenylate tract at its 3' end, and it is flanked by a short direct repeat. These sequences have arisen by different mechanisms, including one that probably involves reverse transcription of a processed messenger RNA and reintegration of the complementary DNA copy into the genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilde, C D -- Crowther, C E -- Cowan, N J -- GM26456/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Aug 6;217(4559):549.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6178164" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; DNA/analysis ; DNA Restriction Enzymes ; DNA Transposable Elements ; DNA, Recombinant ; *Gene Expression Regulation ; Humans ; Nucleic Acid Hybridization ; Poly A/genetics ; RNA Splicing ; RNA-Directed DNA Polymerase/metabolism ; Recombination, Genetic ; Tubulin/*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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    AKTUELLE ARTIKEL
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