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  • Artikel  (25)
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  • American Association for the Advancement of Science (AAAS)  (25)
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  • American Association for the Advancement of Science (AAAS)  (25)
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  • 1
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    Effect of carboxylic acid side chains on the absorption maximum of visual pigments (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1989-11-17
    Beschreibung: The proposal that the absorption maximum of the visual pigments is governed by interaction of the 11-cis-retinal chromophore with charged carboxylic acid side chains in the membrane-embedded regions of the proteins has been tested by mutating five Asp and Glu residues thought to be buried in rhodopsin. Changing Glu113 to Gln causes a dramatic shift in the absorption maximum from 500 nanometers to 380 nanometers, a decrease in the pKa (acidity constant) of the protonated Schiff base of the chromophore to about 6, and a greatly increased reactivity with hydroxylamine. Thus Glu113 appears to be the counterion to the protonated Schiff base. Wavelength modulation in visual pigments apparently is not governed by electrostatic interaction with carboxylate residues, other than the counterion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhukovsky, E A -- Oprian, D D -- 5T32 GM07596-11/GM/NIGMS NIH HHS/ -- EY07965/EY/NEI NIH HHS/ -- R01 EY007965/EY/NEI NIH HHS/ -- S07 RR07044/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1989 Nov 17;246(4932):928-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2573154" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Aspartic Acid ; Glutamates ; Glutamic Acid ; Hydrogen-Ion Concentration ; Hydroxylamine ; Hydroxylamines/pharmacology ; Models, Molecular ; Mutation ; Protein Conformation ; Retinal Pigments/*metabolism ; Retinaldehyde/*metabolism ; Retinoids/*metabolism ; Rhodopsin/genetics/*metabolism ; Schiff Bases ; Spectrophotometry
    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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    Three-dimensional structure of cholera toxin penetrating a lipid membrane (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1988-03-11
    Beschreibung: Two-dimensional crystals of cholera toxin bound to receptors in a lipid membrane give diffraction extending to 15 A resolution. Three-dimensional structure determination reveals a ring of five B subunits on the membrane surface, with one-third of the A subunit occupying the center of the ring. The remaining mass of the A subunit appears to penetrate the hydrophobic interior of the membrane. Cleavage of a disulfide bond in the A subunit, which activates the toxin, causes a major conformational change, with the A subunit mostly exiting from the B ring.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ribi, H O -- Ludwig, D S -- Mercer, K L -- Schoolnik, G K -- Kornberg, R D -- AI21144/AI/NIAID NIH HHS/ -- GM07276-12/GM/NIGMS NIH HHS/ -- GM07365/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Mar 11;239(4845):1272-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3344432" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Cholera Toxin ; G(M1) Ganglioside ; *Liposomes ; Macromolecular Substances ; Microscopy, Electron ; Models, Molecular ; Phosphatidylethanolamines ; 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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  • 3
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    Crystal structure of Cd,Zn metallothionein (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1986-02-14
    Beschreibung: 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〉
    Schlagwort(e): Animals ; Binding Sites ; Cadmium ; Crystallography ; Cysteine ; *Metallothionein ; Models, Molecular ; Protein Conformation ; Rats ; Solutions ; X-Ray Diffraction ; Zinc
    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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    Structure of pressinoic acid: the cyclic moiety of vasopressin (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1986-06-06
    Beschreibung: Arginine vasopressin consists of a 20-membered, disulfide-linked macrocyclic ring system called pressinoic acid to which is attached a COOH-terminal tripeptide. The molecular conformation of pressinoic acid has been determined from single crystal x-ray diffraction data. The 20-membered macrocyclic ring, stabilized by two intramolecular hydrogen bonds, has a type I beta-bend centered on Gln4 and Asn5 and a highly distorted type II' bend centered on Phe3 and Gln4. In vasopressin the Asn5 side chain extends away from the macrocyclic ring system and hydrogen bonds to the terminal tripeptide, but in pressinoic acid the Asn5 side chain lies over the molecule and forms a strong hydrogen bond to the nitrogen of Tyr2. The absence of pressor activity in pressinoic acid may be a result of both the loss of the COOH-terminal tripeptide and the incorrect orientation of the Asn5 side chain. Whether this class of hormones has pressor or oxytocic activity is determined by the orientation of the Tyr2 side chain, that is, whether it is extended away from or over the ring system, respectively. In pressinoic acid, the Tyr2 side chain is in the expected "pressor conformation," that is, extended away from the ring system, and is stabilized through a hydrophobic interaction with the Phe3 side chain. Thus, the conformation of the pressinoic acid molecule partly explains the activity of vasopressin-like hormones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Langs, D A -- Smith, G D -- Stezowski, J J -- Hughes, R E -- GM32812/GM/NIGMS NIH HHS/ -- HL32303/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 6;232(4755):1240-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3704648" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Arginine Vasopressin ; Models, Molecular ; Molecular Conformation ; *Vasopressins ; 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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  • 5
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    Accelerated electron transfer between metal complexes mediated by DNA (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1988-09-23
    Beschreibung: DNA-mediated long-range electron transfer from photoexcited 1,10-phenanthroline complexes of ruthenium, Ru(phen)2(3)+, to isostructural complexes of cobalt(III), rhodium(III), and chromium(III) bound along the helical strand. The efficiency of transfer depended upon binding mode and driving force. For a given donor-acceptor pair, surface-bound complexes showed greater rate enhancements than those that were intercalatively bound. Even in rigid glycerol at 253 K, the rates for donor-acceptor pairs bound to DNA remained enhanced. For the series of acceptors, the greatest enhancement in electron-transfer rate was found with chromium, the acceptor of intermediate driving force. The DNA polymer appears to provide an efficient intervening medium to couple donor and acceptor metal complexes for electron transfer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Purugganan, M D -- Kumar, C V -- Turro, N J -- Barton, J K -- New York, N.Y. -- Science. 1988 Sep 23;241(4873):1645-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Columbia University, New York, NY 10027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3420416" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding, Competitive ; DNA/*metabolism ; Diffusion ; Electron Transport ; Glycerol/metabolism ; Metals/*metabolism ; Models, Molecular ; Phenanthrolines/metabolism ; Ruthenium/metabolism ; Temperature ; Viscosity
    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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    Three-dimensional solution structure of plastocyanin from the green alga Scenedesmus obliquus (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1988-04-15
    Beschreibung: The solution conformation of plastocyanin from the green alga Scenedesmus obliquus has been determined from distance and dihedral angle constraints derived by nuclear magnetic resonance (NMR) spectroscopy. Structures were generated with distance geometry and restrained molecular dynamics calculations. A novel molecular replacement method was also used with the same NMR constraints to generate solution structures of S. obliquus plastocyanin from the x-ray structure of the homologous poplar protein. Scenedesmus obliquus plastocyanin in solution adopts a beta-barrel structure. The backbone conformation is well defined and is similar overall to that of poplar plastocyanin in the crystalline state. The distinctive acidic region of the higher plant plastocyanins, which functions as a binding site for electron transfer proteins and inorganic complexes, differs in both shape and charge in S. obliquus plastocyanin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, J M -- Case, D A -- Chazin, W J -- Gippert, G P -- Havel, T F -- Powls, R -- Wright, P E -- GM36643/GM/NIGMS NIH HHS/ -- GM38221/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):314-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3353725" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Calorimetry ; Chlorophyta/*metabolism ; Magnetic Resonance Spectroscopy/methods ; Models, Molecular ; *Plant Proteins ; *Plastocyanin ; 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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  • 7
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    Structural origins of high-affinity biotin binding to streptavidin (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1989-01-06
    Beschreibung: The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an irreversible and specific linkage between biological macromolecules. Comparison of the refined crystal structures of apo and a streptavidin:biotin complex shows that the high affinity results from several factors. These factors include the formation of multiple hydrogen bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the biotin in the protein interior. Structural alterations at the biotin binding site produce quaternary changes in the streptavidin tetramer. These changes apparently propagate through cooperative deformations in the twisted beta sheets that link tetramer subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, P C -- Ohlendorf, D H -- Wendoloski, J J -- Salemme, F R -- New York, N.Y. -- Science. 1989 Jan 6;243(4887):85-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Central Research & Development Department, E. I. du Pont de Neumours and Company, Inc., Wilmington, DE 19880-0228.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2911722" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bacterial Proteins/*metabolism ; Binding Sites ; Biotin/*metabolism ; Macromolecular Substances ; Models, Molecular ; Protein Conformation ; Streptavidin ; 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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  • 8
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    Structure of recombinant human renin, a target for cardiovascular-active drugs, at 2.5 A resolution (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1989-03-10
    Beschreibung: The x-ray crystal structure of recombinant human renin has been determined. Molecular dynamics techniques that included crystallographic data as a restraint were used to improve an initial model based on porcine pepsinogen. The present agreement factor for data from 8.0 to 2.5 angstroms (A) is 0.236. Some of the surface loops are poorly determined, and these disordered regions border a 30 A wide solvent channel. Comparison of renin with other aspartyl proteinases shows that, although the structural cores and active sites are highly conserved, surface residues, some of which are critical for specificity, vary greatly (up to 10A). Knowledge of the actual structure, as opposed to the use of models based on related enzymes, should facilitate the design of renin inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sielecki, A R -- Hayakawa, K -- Fujinaga, M -- Murphy, M E -- Fraser, M -- Muir, A K -- Carilli, C T -- Lewicki, J A -- Baxter, J D -- James, M N -- New York, N.Y. -- Science. 1989 Mar 10;243(4896):1346-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Alberta, Edmonton, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2493678" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Aspartic Acid Endopeptidases ; Cardiovascular Agents/pharmacology ; Endopeptidases/metabolism ; Humans ; Models, Molecular ; Pepsin A/metabolism ; Protein Conformation ; *Recombinant Proteins/metabolism ; *Renin/metabolism
    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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  • 9
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    Protein design, a minimalist approach (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1989-02-03
    Beschreibung: The question of how the amino acid sequence of a protein specifies its three-dimensional structure remains to be answered. Proteins are so large and complex that it is difficult to discern the features in their sequences that contribute to their structural stability and function. One approach to this problem is de novo design of model proteins, much simpler than their natural counterparts, yet containing sufficient information in their sequences to specify a given function (for example, folding in aqueous solution, folding in membranes, or formation of ion channels). Designed proteins provide simple model systems for understanding protein structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeGrado, W F -- Wasserman, Z R -- Lear, J D -- New York, N.Y. -- Science. 1989 Feb 3;243(4891):622-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉E. I. du Pont de Nemours & Company, Central Research and Development Department, Wilmington, DE 19898.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2464850" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Ion Channels ; Macromolecular Substances ; Models, Molecular ; Protein Conformation ; *Proteins ; Solubility ; Structure-Activity Relationship ; Tropomyosin ; Water
    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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  • 10
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    A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1988-12-16
    Beschreibung: Three variations to the structure of the nicotinamide adenine dinucleotide (NAD)-dependent L-lactate dehydrogenase from Bacillus stearothermophilus were made to try to change the substrate specificity from lactate to malate: Asp197----Asn, Thr246----Gly, and Gln102----Arg). Each modification shifts the specificity from lactate to malate, although only the last (Gln102----Arg) provides an effective and highly specific catalyst for the new substrate. This synthetic enzyme has a ratio of catalytic rate (kcat) to Michaelis constant (Km) for oxaloacetate of 4.2 x 10(6)M-1 s-1, equal to that of native lactate dehydrogenase for its natural substrate, pyruvate, and a maximum velocity (250 s-1), which is double that reported for a natural malate dehydrogenase from B. stearothermophilus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilks, H M -- Hart, K W -- Feeney, R -- Dunn, C R -- Muirhead, H -- Chia, W N -- Barstow, D A -- Atkinson, T -- Clarke, A R -- Holbrook, J J -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1541-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Bristol, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201242" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Geobacillus stearothermophilus/*enzymology/genetics ; Kinetics ; L-Lactate Dehydrogenase/*genetics/metabolism ; Malate Dehydrogenase/*metabolism ; Models, Molecular ; Protein Conformation ; Substrate Specificity
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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