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  • 1985-1989  (342)
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  • 1
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    U.s. Scientists and china (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-12-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, J C -- New York, N.Y. -- Science. 1989 Dec 22;246(4937):1547.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17834400" target="_blank"〉PubMed〈/a〉
    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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    Action at a distance along a DNA (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-15
    Description: A number of ways are known by which an event at one location on a DNA molecule can affect an event at a distant location on the same molecule. Three classes of mechanisms are described for such distal actions: tracking or translocation of a protein along a DNA, the association of two proteins bound at separate sites to form a DNA loop in between, and distal interactions that are affected by the topology of the DNA. The basic characteristics of each type of mechanism are discussed in terms of the known physicochemical properties of DNA. The various modes of action at a distance are often interrelated. Examples include the formation of positively and negatively supercoiled DNA loops by tracking and the strong effects of DNA topology on looping.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, J C -- Giaever, G N -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):300-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3281259" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA/genetics/metabolism ; DNA, Superhelical ; Deoxyribonucleoproteins/metabolism ; Models, Molecular ; *Nucleic Acid Conformation
    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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    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
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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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
    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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    Tandem regions of yeast DNA topoisomerase II share homology with different subunits of bacterial gyrase (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-08
    Description: The nucleotide sequence for the Saccharomyces cerevisiae gene TOP2, which encodes DNA topoisomerase II, was compared with the sequence for bacterial DNA gyrase. The amino and carboxyl terminal halves of the single-subunit yeast enzyme showed homologies with the B and A subunits of bacterial gyrase, respectively, at corresponding positions along the polypeptide chains. Although the two enzymes differ in both quaternary structure and activity, the homology between the two proteins indicates mechanistic as well as structural similarities, and a probable evolutionary relationship.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lynn, R -- Giaever, G -- Swanberg, S L -- Wang, J C -- GM24544/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 8;233(4764):647-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014661" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/enzymology/genetics ; DNA Topoisomerases, Type II/*genetics ; Escherichia coli/enzymology/genetics ; Genes, Fungal ; Saccharomyces cerevisiae/enzymology/*genetics ; Sequence Homology, Nucleic Acid
    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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  • 6
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    Structure of the DNA-Eco RI endonuclease recognition complex at 3 A resolution (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-19
    Description: The crystal structure of the complex between Eco RI endonuclease and the cognate oligonucleotide TCGCGAATTCGCG provides a detailed example of the structural basis of sequence-specific DNA-protein interactions. The structure was determined, to 3 A resolution, by the ISIR (iterative single isomorphous replacement) method with a platinum isomorphous derivative. The complex has twofold symmetry. Each subunit of the endonuclease is organized into an alpha/beta domain consisting a five-stranded beta sheet, alpha helices, and an extension, called the "arm," which wraps around the DNA. The large beta sheet consists of antiparallel and parallel motifs that form the foundations for the loops and alpha helices responsible for DNA strand scission and sequence-specific recognition, respectively. The DNA cleavage site is located in a cleft that binds the DNA backbone in the vicinity of the scissile bond. Sequence specificity is mediated by 12 hydrogen bonds originating from alpha helical recognition modules. Arg200 forms two hydrogen bonds with guanine while Glu144 and Arg145 form four hydrogen bonds to adjacent adenine residues. These interactions discriminate the Eco RI hexanucleotide GAATTC from all other hexanucleotides because any base substitution would require rupture of at least one of these hydrogen bonds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McClarin, J A -- Frederick, C A -- Wang, B C -- Greene, P -- Boyer, H W -- Grable, J -- Rosenberg, J M -- GM25671/GM/NIGMS NIH HHS/ -- GM33506/GM/NIGMS NIH HHS/ -- RR07084/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1526-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3024321" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/metabolism ; Base Composition ; Binding Sites ; Chemistry, Physical ; Crystallization ; DNA/*metabolism ; DNA Restriction Enzymes/*metabolism ; Deoxyribonuclease EcoRI ; Hydrogen Bonding ; Macromolecular Substances ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/metabolism ; Physicochemical Phenomena ; Protein Conformation ; Substrate Specificity
    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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  • 7
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    Antarctic stratospheric chemistry of chlorine nitrate, hydrogen chloride, and ice: release of active chlorine (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-11-27
    Description: The reaction rate between atmospheric hydrogen chloride (HCl) and chlorine nitrate (ClONO(2)) is greatly enhanced in the presence of ice particles; HCl dissolves readily into ice, and the collisional reaction probability for ClONO(2) on the surface of ice with HCl in the mole fraction range from approximately 0.003 to 0.010 is in the range from approximately 0.05 to 0.1 for temperatures near 200 K. Chlorine (Cl(2)) is released into the gas phase on a time scale of at most a few milliseconds, whereas nitric acid (HNO(3)), the other product, remains in the condensed phase. This reaction could play an important role in explaining the observed depletion of ozone over Antarctica; it releases photolytically active chlorine from its most abundant reservoir species, and it promotes the formation of HNO(3) and thus removes nitrogen dioxide (NO(2)) from the gas phase. Hence it establishes the necessary conditions for the efficient catalytic destruction of ozone by halogenated free radicals. In the absence of HCl, ClONO(2) also reacts irreversibly with ice with a collision efficiency of approximately 0.02 at 200 K; the product hypochlorous acid (HOCI) is released to the gas phase on a time scale of minutes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Molina, M J -- Tso, T L -- Molina, L T -- Wang, F C -- New York, N.Y. -- Science. 1987 Nov 27;238(4831):1253-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17744362" target="_blank"〉PubMed〈/a〉
    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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  • 8
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    Crystal structure of Cd,Zn metallothionein (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-02-14
    Description: The anomalous scattering data from five Cd in the native protein were used to determine the crystal structure of cadmium, zinc (Cd,Zn) metallothionein isoform II from rat liver. The structure of a 4-Cd cluster was solved by direct methods. A 2.3 A resolution electron density map was calculated by iterative single-wavelength anomalous scattering. The structure is folded into two domains. The amino terminal domain (beta) of residues 1 to 29 enfolds a three-metal cluster of one Cd and two Zn atoms coordinated by six terminal cysteine thiolate ligands and three bridging cysteine thiolates. The carboxyl terminal domain (alpha) of residues 30 to 61 enfolds a 4-Cd cluster coordinated by six terminal and five bridging cysteine thiolates. All seven metal sites have tetrahedral coordination geometry. The domains are roughly spherical, and the diameter is 15 to 20 A; there is limited contact between domains. The folding of alpha and beta is topologically similar but with opposite chirality. Redundant, short cysteine-containing sequences have similar roles in cluster formation in both alpha and beta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Furey, W F -- Robbins, A H -- Clancy, L L -- Winge, D R -- Wang, B C -- Stout, C D -- GM-36535/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 14;231(4739):704-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3945804" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cadmium ; Crystallography ; Cysteine ; *Metallothionein ; Models, Molecular ; Protein Conformation ; Rats ; Solutions ; X-Ray Diffraction ; Zinc
    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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  • 9
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    Crystallographic structure of the octamer histone core of the nucleosome (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moudrianakis, E N -- Love, W E -- Wang, B C -- Xuong, N G -- Burlingame, R W -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1110-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17753284" target="_blank"〉PubMed〈/a〉
    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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  • 10
    Electronic Resource
    Electronic Resource
    Investigation of the mass diffusion of camphorquinone in amorphous poly(methyl methacrylate) and poly(tert-butyl methacrylate) hosts by the induced holographic grating relaxation technique (1986)
    s.l. : American Chemical Society
    Macromolecules 19 (1986), S. 1390-1394 
    Details
    ISSN: 1520-5835
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ma00159a018
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    Paper (German National Licenses)
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