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  • Chemistry  (50,842)
  • Science
  • 1990-1994  (50,858)
  • 1
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    All-women conference: did it discriminate? (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galloway, A -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1319.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2078250" target="_blank"〉PubMed〈/a〉
    Keywords: *Congresses as Topic ; Female ; Government Agencies ; Humans ; *Prejudice ; Science ; United States ; *Women
    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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    A base dispute (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waldrop, M M -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):472-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2382127" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; *Information Systems ; Jurisprudence ; Societies, Scientific ; United States
    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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    Clathrate hydrate formation in amorphous cometary ice analogs in vacuo (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: The presence of clathrate hydrates in cometary ice has been suggested to account for anomalous gas release at large radial distances from the sun as well as the retention of volatiles in comets to elevated temperatures. However, how clathrate hydrates can form in low-pressure environments, such as in cold interstellar molecular clouds, in the outer reaches of the early solar nebula, or in cometary ices, has been poorly understood. Experiments performed with the use of a modified electron microscope demonstrate that during the warming of vapor-deposited amorphous ices in vacuo, clathrate hydrates can form by rearrangements in the solid state. Phase separations and microporous textures that are the result of these rearrangements may account for a variety of anomalous cometary phenomena.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blake, D -- Allamandola, L -- Sandford, S -- Hudgins, D -- Freund, F -- New York, N.Y. -- Science. 1991 Oct 25;254:548-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Planetary Biology Branch, Ames Research Center, Moffett Field, CA 94035, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11538372" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Crystallography ; Earth (Planet) ; Hydrocarbons/chemistry ; Ice/*analysis ; *Meteoroids ; Microscopy, Electron ; *Solar System
    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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    Direct measurement of forces between linear polysaccharides xanthan and schizophyllan (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-14
    Description: Direct osmotic stress measurements have been made of forces between helices of xanthan, an industrially important charged polysaccharide. Exponentially decaying hydration forces, much like those already measured between lipid bilayer membranes or DNA double helices, dominate the interactions at close separation. Interactions between uncharged schizophyllans also show the same kind of hydration force seen between xanthans. In addition to the practical possibilities for modifying solution and suspension properties through recognition and control of molecular forces, there is now finally the opportunity for theorists to relate macroscopic properties of a polymer solution to the microscopic properties that underlie them.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rau, D C -- Parsegian, V A -- New York, N.Y. -- Science. 1990 Sep 14;249(4974):1278-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases, National Institues of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2144663" target="_blank"〉PubMed〈/a〉
    Keywords: Carbohydrate Sequence ; Chemical Phenomena ; Chemistry ; Gels ; *Glycosaminoglycans ; Macromolecular Substances ; Molecular Sequence Data ; Osmosis ; *Polysaccharides, Bacterial ; *Sizofiran ; Solutions ; Viscosity
    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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    Common features of protein unfolding and dissolution of hydrophobic compounds (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-02-02
    Description: Protein unfolding and the dissolution of hydrophobic compounds (including solids, liquids, and gases) in water are characterized by a linear relation between entropy change and heat capacity change. The same slope is found for various classes of compounds, whereas the intercept depends on the particular class. The feature common to these processes is exposure of hydrophobic groups to water. These observations make possible the assignment of the heat capacity change to hydrophobic solvation and lead to the description of protein stability in terms of a hydrophobic and a nonhydrophobic contribution. A general representation of protein stability is given by the heat capacity change and the temperature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphy, K P -- Privalov, P L -- Gill, S J -- New York, N.Y. -- Science. 1990 Feb 2;247(4942):559-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2300815" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; *Protein Denaturation ; *Proteins ; Thermodynamics
    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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    Interparticle collisions driven by ultrasound (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-02
    Description: Ultrasound has become an important synthetic tool in liquid-solid chemical reactions, but the origins of the observed enhancements remained unknown. The effects of high-intensity ultrasound on solid-liquid slurries were examined. Turbulent flow and shock waves produced by acoustic cavitation were found to drive metal particles together at sufficiently high velocities to induce melting upon collision. A series of transition-metal powders were used to probe the maximum temperatures and speeds reached during such interparticle collisions. Metal particles that were irradiated in hydrocarbon liquids with ultrasound underwent collisions at roughly half the speed of sound and generated localized effective temperatures between 2600 degrees C and 3400 degrees C at the point of impact for particles with an average diameter of approximately 10 microns.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doktycz, S J -- Suslick, K S -- New York, N.Y. -- Science. 1990 Mar 2;247(4946):1067-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Chemical Sciences, University of Illinois, Urbana 61801.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2309118" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; *Metals ; Microscopy, Electron, Scanning ; Microspheres ; *Ultrasonics
    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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    Changes in mean concentration, phase shifts, and dissipation in a forced oscillatory reaction (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-01-12
    Description: Experiments are presented that confirm earlier predictions that the mode of supply of reactants to a nonlinear (bio)chemical reaction determines or controls concentrations at steady states far from equilibrium. The oxidation of nicotinamide adenine dinucleotide (NADH) catalyzed by the enzyme horseradish peroxidase with continuous input of oxygen was studied; NAD+ is continuously recycled to NADH through a glucose-6-phosphate dehydrogenase system. A comparison of steady-state concentrations is made with an oscillatory oxygen input and a constant input at the same average oxygen input for both modes. By varying the frequency and amplitude of the perturbation (O2 influx), the following may be changed: the average concentration of NADH; the Gibbs free energy difference delta G of the reactants and products at steady state; the average rate of the reaction; the phase relation between the oscillatory rate and delta G; and the dissipation. These results confirm the possibility of an "alternating current chemistry," of control and optimization of thermodynamic efficiency and dissipation by means of external variation of constraints in classes of nonlinear reactions and biological pumps, and of improvements of the yield in such reactions (heterogeneous catalysis, for example).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lazar, J G -- Ross, J -- New York, N.Y. -- Science. 1990 Jan 12;247(4939):189-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2294601" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Chemical Phenomena ; Chemistry ; Glucosephosphate Dehydrogenase/*metabolism ; Horseradish Peroxidase/*metabolism ; Kinetics ; NAD/*metabolism ; Oxidation-Reduction ; Oxygen/metabolism ; Peroxidases/*metabolism ; Thermodynamics
    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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    An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-17
    Description: The interaction of a protein antigen, horse cytochrome c (cyt c), with a monoclonal antibody has been studied by hydrogen-deuterium (H-D) exchange labeling and two-dimensional nuclear magnetic resonance (2D NMR) methods. The H-exchange rate of residues in three discontiguous regions of the cyt c polypeptide backbone was slowed by factors up to 340-fold in the antibody-antigen complex compared with free cyt c. The protected residues, 36 to 38, 59, 60, 64 to 67, 100, and 101, and their hydrogen-bond acceptors, are brought together in the three-dimensional structure to form a contiguous, largely exposed protein surface with an area of about 750 square angstroms. The interaction site determined in this way is consistent with prior epitope mapping studies and includes several residues that were not previously identified. The hydrogen exchange labeling approach can be used to map binding sites on small proteins in antibody-antigen complexes and may be applicable to protein-protein and protein-ligand interactions in general.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432411/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432411/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paterson, Y -- Englander, S W -- Roder, H -- GM 31847/GM/NIGMS NIH HHS/ -- GM 35926/GM/NIGMS NIH HHS/ -- R01 GM031847/GM/NIGMS NIH HHS/ -- S07-RR-05415-28/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):755-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Pennsylvania, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1697101" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal/immunology/metabolism ; Antigen-Antibody Complex ; *Binding Sites, Antibody ; Chemical Phenomena ; Chemistry ; Cytochrome c Group/*immunology ; Deuterium ; Epitopes/immunology ; Hydrogen/*metabolism ; Hydrogen Bonding ; Kinetics ; *Magnetic Resonance Spectroscopy ; Molecular Structure ; Protein Conformation
    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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    Manifest destiny at the Scripps Research Institute (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baskin, Y -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):140-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1853198" target="_blank"〉PubMed〈/a〉
    Keywords: *Academies and Institutes ; Biology ; California ; Chemical Phenomena ; Chemistry ; Research Support as Topic
    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
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    NSF holds plan close to its vest (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):872.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502550" target="_blank"〉PubMed〈/a〉
    Keywords: Government Agencies/*organization & administration ; National Institutes of Health (U.S.)/organization & administration ; Science ; United States
    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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