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  • Models, Molecular
  • American Association for the Advancement of Science (AAAS)  (9)
  • 1980-1984  (9)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (9)
Years
Year
  • 1
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    Bimolane: structure determination indicates anticancer activity is attributable to ICRF-154 (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-14
    Description: X-ray diffraction studies of crystals from samples of bimolane synthesized in China and in the United States showed that the crystals consist of the related compound ICRF-154. Analysis of the results of biological tests did not show any significant differences between the anticancer activity of bimolane and ICRF-154. It appears that the anticancer activity of bimolane is due to ICRF-154.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Camerman, N -- Hempel, A -- Camerman, A -- CA 15879/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 14;225(4667):1165-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474171" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents/*pharmacology ; Models, Molecular ; *Piperazines ; *Razoxane/analogs & derivatives ; 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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  • 2
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    Conformational variability of NAD+ in the free and bound states: a nicotinamide sandwich in NAD+ crystals (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-23
    Description: X-ray analysis of the free-acid crystal form of the coenzyme nicotinamide adenine dinucleotide (NAD+) revealed a conformational difference between the free NAD+ molecule and one bound in enzymes or complexed to Li+ ions. The pyrophosphate group showed asymmetry in the phosphate-oxygen bonds of the phosphate-oxygen-phosphate link; this bond at the nicotinamide side of the link is longer than that at the adenosine side by 0.04 angstrom. The crystal structure showed a novel intermolecular stacking of adenine and water molecules on opposite sides of nicotinamide that gives rise to a nicotinamide sandwich.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parthasarathy, R -- Fridey, S M -- GM-24864/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):969-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6239374" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohol Dehydrogenase ; Alcohol Oxidoreductases/metabolism ; Animals ; Geobacillus stearothermophilus/enzymology ; Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism ; L-Lactate Dehydrogenase/metabolism ; Liver/enzymology ; Malate Dehydrogenase/metabolism ; Models, Molecular ; Molecular Conformation ; *NAD/metabolism ; Nephropidae ; Niacinamide ; Protein Binding ; 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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  • 3
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    The molecular structure of a DNA-triostin A complex (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-14
    Description: The molecular structure of triostin A, a cyclic octadepsipeptide antibiotic, has been solved complexed to a DNA double helical fragment with the sequence CGTACG (C, cytosine; G, guanine; T, thymine; A, adenine). The two planar quinoxaline rings of triostin A bis intercalate on the minor groove of the DNA double helix surrounding the CG base pairs at either end. The alanine residues form hydrogen bonds to the guanines. Base stacking in the DNA is perturbed, and the major binding interaction involves a large number of van der Waals contacts between the peptides and the nucleic acid. The adenine residues in the center are in the syn conformation and are paired to thymine through Hoogsteen base pairing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A H -- Ughetto, G -- Quigley, G J -- Hakoshima, T -- van der Marel, G A -- van Boom, J H -- Rich, A -- New York, N.Y. -- Science. 1984 Sep 14;225(4667):1115-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474168" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; DNA/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; Quinoxalines/metabolism
    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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    Protein engineering (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-02-11
    Description: 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〉
    Keywords: Base Sequence ; Crystallography ; Genes ; *Genetic Engineering ; Models, Molecular ; Molecular Biology/trends ; Protein Conformation ; Proteins/*genetics ; 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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  • 5
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    The anatomy of A-, B-, and Z-DNA (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-04-30
    Description: Recent advances in DNA synthesis methods have made it possible to carry out single-crystal x-ray analyses of double-stranded DNA molecules of predetermined sequence, with 4 to 12 base pairs. At least one example has been examined from each of the three known families of DNA helix: A, B, and Z. Each family has its own intrinsic restrictions on chain folding and structure. The observed solvent positions in these crystal structures have confirmed earlier fiber and solution measurements, and have led to proposals explaining the transitions from B to A and from B to Z helices. Prospects are improving for an understanding of the mode of bending of DNA in chromatin, and the way in which specific DNA sequences are recognized by drug molecules and repressor proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dickerson, R E -- Drew, H R -- Conner, B N -- Wing, R M -- Fratini, A V -- Kopka, M L -- New York, N.Y. -- Science. 1982 Apr 30;216(4545):475-85.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7071593" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography ; *Dna ; Hydrogen Bonding ; Models, Molecular ; Nucleic Acid 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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  • 6
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    Penicillin target enzyme and the antibiotic binding site (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-29
    Description: 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〉
    Keywords: Binding Sites ; *Carboxypeptidases ; *Cephalosporins ; Crystallography ; Models, Molecular ; *Muramoylpentapeptide Carboxypeptidase ; *Penicillins ; 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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  • 7
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    Diameter of the cell-to-cell junctional membrane channels as probed with neutral molecules (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-07-31
    Description: The cell-to-cell channels in the junctions of an insect salivary gland and of insect and mammalian cells in culture were probed with fluorescent molecules-neutral linear oligosaccharides, neutral branched glycopeptides, and charged linear peptides. From the molecular dimensions of the largest permeants and smallest impermeants the permeation-limiting channel diameter was obtained: 16 to 20 angstroms for the mammalian cells and 20 to 30 angstroms for the insect cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwarzmann, G -- Wiegandt, H -- Rose, B -- Zimmerman, A -- Ben-Haim, D -- Loewenstein, W R -- CA 14464/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 31;213(4507):551-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7244653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chironomidae ; Fluorescent Dyes ; Glycopeptides/*metabolism ; Intercellular Junctions/*ultrastructure ; Mice ; Mice, Inbred BALB C ; Models, Molecular ; Oligosaccharides/*metabolism ; Protein Conformation ; Salivary Glands/*ultrastructure ; Species 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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  • 8
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    Left-handed double helical DNA: variations in the backbone conformation (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-01-09
    Description: Four different crystals of d(CpGpCpGpCpG) have been solved by x-ray diffraction analysis and all form similar left-handed double helical Z-DNA molecules in the crystal lattice. Two different conformations are observed for the phosphates in the GpC sequences, as the phosphates are found either facing the helical groove or rotated away from it. The latter conformation is often found when hydrated magnesium ions are complexed to a phosphate oxygen atom. These different conformations may be used when right-handed B-DNA joins left-handed Z-DNA. Atomic coordinates and torsion angles are presented for both types of Z-DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A J -- Quigley, G J -- Kolpak, F J -- van der Marel, G -- van Boom, J H -- Rich, A -- New York, N.Y. -- Science. 1981 Jan 9;211(4478):171-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444458" target="_blank"〉PubMed〈/a〉
    Keywords: *Dna ; Fourier Analysis ; Hydrogen Bonding ; Magnesium ; Models, Molecular ; *Nucleic Acid Conformation ; Oligodeoxyribonucleotides ; Spermine ; 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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  • 9
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    Deoxyribonucleic acid structure: a new model (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-01-16
    Description: Models of deoxyribonucleic acid (DNA) having chain directions opposite to those of the Watson and Crick model offer strikingly different alternatives for DNA structures. Satisfactory models of the B and C forms of DNA have been built. Left-handed models readily form by twisting right-handed ones, and models can be bent into tight supercoils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hopkins, R C -- New York, N.Y. -- Science. 1981 Jan 16;211(4479):289-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444467" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/ultrastructure ; *Dna ; 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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