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  • Articles: DFG German National Licenses  (3)
  • 1990-1994  (3)
  • Chemistry  (3)
  • 1
    Electronic Resource
    Electronic Resource
    The enzymatic mechanism of carboxypeptidase: A molecular dynamics study (1994)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 18 (1994), S. 186-197 
    Details
    ISSN: 0887-3585
    Keywords: carboxypeptidas ; molecular dynamics ; enzymatic mechanisms ; peptidase mechanism ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: An MD simulation of the system carboxypeptidase A (CPA) with the tetrapeptide Val-Leu-Phe-Phe has been performed in order to learn about the substrate disposition just prior to nucleophilic attack. We have explored the model in which the substrate does not substitute the zinc-coordinated water (the “water” mechanism). The simulations do suggest as feasible that the Zn-OH2 group performs a nucleophilic attack on the Phe-Phe peptidic bond. We have also investigated the model in which the carbonyl oxygen displaces the zinc-coordinated water. In this case the substrate and Glu-270 orient themselves to allow an anhydride intermediate during the peptidic bond cleavage (the “anhydride” mechanism). Based on the results of the simulations, both “water” and “anhydride” mechanisms are structurally feasible, although the former model seems more probable on chemical grounds. © 1994 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340180210
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Guest editor's foreword (1993)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 31 (1993), S. S1 
    Details
    ISSN: 0749-1581
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260311302
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Copper-cobalt superoxide dismutase: A re-examination of the 1H NMR spectrum through a novel selectively deuteriated derivative (1993)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 31 (1993), S. S17 
    Details
    ISSN: 0749-1581
    Keywords: 1H NMR ; Copper-cobalt dismutase ; 1D-NOESY ; 2D-NOESY ; T1 measurements ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Through 1D and 2D NOESY experiments, samples of copper-cobalt superoxide dismutase in which the histidines had been completely deuteriated except for the β-CH2 protons were investigated. In this way a simplified spectrum was obtained which allowed the detection of the His NHs of the cobalt domain and their assignment through the kinetics of the proton-deuterium exchange. Further, the β-CH2 protons of Asp 83 were stereospecifically assigned through T1 measurements. Some backbone protons were also assigned.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260311306
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    Paper (German National Licenses)
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