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  • 1
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    Watching a protein as it functions with 150-ps time-resolved x-ray crystallography (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-21
    Description: We report picosecond time-resolved x-ray diffraction from the myoglobin (Mb) mutant in which Leu29 is replaced by Phe (L29Fmutant). The frame-by-frame structural evolution, resolved to 1.8 angstroms, allows one to literally "watch" the protein as it executes its function. Time-resolved mid-infrared spectroscopy of flash-photolyzed L29F MbCO revealed a short-lived CO intermediate whose 140-ps lifetime is shorter than that found in wild-type protein by a factor of 1000. The electron density maps of the protein unveil transient conformational changes far more dramatic than the structural differences between the carboxy and deoxy states and depict the correlated side-chain motion responsible for rapidly sweeping CO away from its primary docking site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schotte, Friedrich -- Lim, Manho -- Jackson, Timothy A -- Smirnov, Aleksandr V -- Soman, Jayashree -- Olson, John S -- Phillips, George N Jr -- Wulff, Michael -- Anfinrud, Philip A -- AR40252/AR/NIAMS NIH HHS/ -- GM35649/GM/NIGMS NIH HHS/ -- HL47020/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2003 Jun 20;300(5627):1944-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12817148" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Binding Sites ; Carbon Monoxide/chemistry/metabolism ; Crystallography, X-Ray/*methods ; Fourier Analysis ; Heme/chemistry ; Ligands ; Models, Molecular ; Mutagenesis, Site-Directed ; Myoglobin/*chemistry/genetics/*metabolism ; Photolysis ; Protein Conformation ; Spectrophotometry, Infrared ; Time Factors ; Whales
    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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    Ultrafast x-ray diffraction of transient molecular structures in solution (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-16
    Description: We report direct structural evidence of the bridged radical (CH2ICH2.) in a polar solution, obtained using time-resolved liquid-phase x-ray diffraction. This transient intermediate has long been hypothesized to explain stereo-chemical control in many association and/or dissociation reactions involving haloalkanes. Ultrashort optical pulses were used to dissociate an iodine atom from the haloethane molecule (C2H4I2) dissolved in methanol, and the diffraction of picosecond x-ray pulses from a synchrotron supports the following structural dynamics, with approximately 0.01 angstrom spatial resolution and approximately 100 picosecond time resolution: The loss of one iodine atom from C2H4I2 leads to the C-I-C triangular geometry of CH2ICH2.. This transient C2H4I then binds to an iodine atom to form a new species, the C2H4I-I isomer, which eventually decays into C2H4 + I2. Solvent dynamics were also extracted from the data, revealing a change in the solvent cage geometry, heating, and thermal expansion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ihee, H -- Lorenc, M -- Kim, T K -- Kong, Q Y -- Cammarata, M -- Lee, J H -- Bratos, S -- Wulff, M -- New York, N.Y. -- Science. 2005 Aug 19;309(5738):1223-7. Epub 2005 Jul 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and School of Molecular Science (BK21), Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 305-701, Republic of Korea. hyotcherl.ihee@kaist.ac.kr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020695" target="_blank"〉PubMed〈/a〉
    Keywords: Computer Simulation ; Free Radicals ; Hydrocarbons, Iodinated/*chemistry ; Isomerism ; Methanol/chemistry ; Molecular Structure ; Scattering, Radiation ; Solutions ; Solvents/chemistry ; Synchrotrons ; Temperature ; Thermodynamics ; Time Factors ; X-Ray Diffraction/*methods ; X-Rays
    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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    Photolysis of the carbon monoxide complex of myoglobin: nanosecond time-resolved crystallography (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: The biological activity of macromolecules is accompanied by rapid structural changes. The photosensitivity of the carbon monoxide complex of myoglobin was used at the European Synchrotron Radiation Facility to obtain pulsed, Laue x-ray diffraction data with nanosecond time resolution during the process of heme and protein relaxation after carbon monoxide photodissociation and during rebinding. These time-resolved experiments reveal the structures of myoglobin photoproducts, provide a structural foundation to spectroscopic results and molecular dynamics calculations, and demonstrate that time-resolved macromolecular crystallography can elucidate the structural bases of biochemical mechanisms on the nanosecond time scale.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Srajer, V -- Teng, T -- Ursby, T -- Pradervand, C -- Ren, Z -- Adachi, S -- Schildkamp, W -- Bourgeois, D -- Wulff, M -- Moffat, K -- GM 36452/GM/NIGMS NIH HHS/ -- RR 07707/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1726-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology and the Consortium for Advanced Radiation Sources, University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939867" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon Monoxide/chemistry/metabolism ; Computer Simulation ; Crystallography, X-Ray/*methods ; Fourier Analysis ; Globins/chemistry ; Heme/chemistry ; Histidine/chemistry ; Iron/chemistry ; Ligands ; Myoglobin/*chemistry/metabolism ; Photolysis ; Temperature ; Time Factors
    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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