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  • Artikel  (7)
  • Protein Conformation
  • American Association for the Advancement of Science (AAAS)  (7)
  • Annual Reviews
  • 2000-2004
  • 1980-1984  (7)
  • 1965-1969
  • 1955-1959
  • 1983  (7)
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  • Artikel  (7)
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Verlag/Herausgeber
  • American Association for the Advancement of Science (AAAS)  (7)
  • Annual Reviews
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  • 2000-2004
  • 1980-1984  (7)
  • 1965-1969
  • 1955-1959
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  • 1
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    Splice junctions: association with variation in protein structure (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1983-06-10
    Beschreibung: 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〉
    Schlagwort(e): 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
    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)
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  • 2
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    Monoclonal antibodies reveal the structural basis of antibody diversity (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1983-11-18
    Beschreibung: 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〉
    Schlagwort(e): 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
    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)
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  • 3
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    Protein engineering (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1983-02-11
    Beschreibung: 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〉
    Schlagwort(e): Base Sequence ; Crystallography ; Genes ; *Genetic Engineering ; Models, Molecular ; Molecular Biology/trends ; Protein Conformation ; Proteins/*genetics ; 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)
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  • 4
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    Waterlogged molecules (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1983-12-09
    Beschreibung: 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〉
    Schlagwort(e): Chemistry, Organic ; Enzymes/physiology ; Kinetics ; Metabolism ; Nucleic Acid Conformation ; Nucleic Acids/physiology ; Organic Chemistry Phenomena ; Protein Conformation ; Solvents ; Water/*physiology
    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)
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  • 5
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    Genes of the major histocompatibility complex in mouse and man (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1983-11-18
    Beschreibung: 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〉
    Schlagwort(e): 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
    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)
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  • 6
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    Fourier transform infrared difference spectra of intermediates in rhodopsin bleaching (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1983-03-18
    Beschreibung: 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〉
    Schlagwort(e): Animals ; Cattle ; Fourier Analysis ; Protein Conformation ; *Retinal Pigments ; *Rhodopsin ; Spectrophotometry, Infrared ; *Vision, Ocular
    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)
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  • 7
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    DNA-binding proteins (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1983-09-09
    Beschreibung: 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〉
    Schlagwort(e): Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; *DNA Helicases ; DNA-Binding Proteins ; Escherichia coli/genetics ; Gene Expression Regulation ; Models, Chemical ; 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)
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