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  • 1H NMR  (2)
  • Analytical Chemistry and Spectroscopy  (2)
  • molecular dynamics  (2)
  • 1
    Digitale Medien
    Digitale Medien
    A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase (1994)
    Springer
    European biophysics journal 23 (1994), S. 167-176 
    Details
    ISSN: 1432-1017
    Schlagwort(e): Cu ; Zn ; Superoxide Dismutase ; 1H NMR ; Monomeric analog
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Physik
    Notizen: Abstract A mutated protein of human Cu(II)2Zn(II)2 SOD in which residues Phe50 and Gly51 at the dimer interface were substituted by Glu's, thus producing a monomeric species, has been characterized by electronic absorption spectroscopy, EPR, relaxivity and1H NMR techniques. Such substitutions and/or accompanying remodeling and exposure of the dimer interface to solvent, alter the geometry of the active site: increases in the axiality of the copper chromophore and the Cu-OH2 distance have been observed. The affinity of both metal binding sites for Co(II) is also altered. The observed NMR parameters of the Co(II) substituted derivative have been interpreted as a function of the decrease of rotational correlation time as a consequence of the lower molecular weight of the mutated protein. Sharper NMR signals are also obtained for the reduced diamagnetic enzyme. Results are consistent with an active site structure similar to that observed for the dimeric analog Thr137Ile characterized elsewhere. An observed proportional decrease in enzymatic activity and affinity for the N3-anion suggests the importance of electrostatic forces during substrate docking and catalysis.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01007608
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  • 2
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): carboxypeptidas ; molecular dynamics ; enzymatic mechanisms ; peptidase mechanism ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: 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.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/prot.340180210
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  • 3
    Digitale Medien
    Digitale Medien
    Pseudocontact shifts as constraints for energy minimization and molecular dynamics calculations on solution structures of paramagnetic metalloproteins (1997)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 29 (1997), S. 68-76 
    Details
    ISSN: 0887-3585
    Schlagwort(e): pseudocontact shifts ; structure calculations ; restrained energy minimization ; molecular dynamics ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: The pseudocontact shifts of NMR signals, which arise from the magnetic susceptibility anisotropy of paramagnetic molecules, have been used as structural constraints under the form of a pseudopotential in the SANDER module of the AMBER 4.1 molecular dynamics software package. With this procedure, restrained energy minimization (REM) and restrained molecular dynamics (RMD) calculations can be performed on structural models by using pseudocontact shifts. The structure of the cyanide adduct of the Met80Ala mutant of the yeast iso-1-cytochrome c has been used for successfully testing the calculations. For this protein, a family of structures is available, which was obtained by using NOE and pseudocontact shifts as constraints in a distance geometry program. The structures obtained by REM and RMD calculations with the inclusion of pseudocontact shifts are analyzed. Proteins 29:68-76, 1997. © 1997 Wiley-Liss, Inc.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
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  • 4
    Digitale Medien
    Digitale Medien
    Guest editor's foreword (1993)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 31 (1993), S. S1 
    Details
    ISSN: 0749-1581
    Schlagwort(e): Chemistry ; Analytical Chemistry and Spectroscopy
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/mrc.1260311302
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  • 5
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): 1H NMR ; Copper-cobalt dismutase ; 1D-NOESY ; 2D-NOESY ; T1 measurements ; Chemistry ; Analytical Chemistry and Spectroscopy
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: 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.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/mrc.1260311306
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