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  • 1
    Digitale Medien
    Digitale Medien
    1H-NMR and relaxometry of copper-containing dimers in proteins (1990)
    Springer
    BioMetals 3 (1990), S. 146-150 
    Details
    ISSN: 1572-8773
    Schlagwort(e): Copper ; Cobalt ; Nickel ; Superoxide dismutase ; Alkaline phosphatase ; NMR ; Relaxometry ; Nuclear relaxation ; Electronic relaxation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Summary The water-proton nuclear-magnetic-relaxation dispersion profiles have been analyzed for Cu2Zn2-superoxide dismutase (SOD) and Cu2-alkaline phosphatase (AP). The electronic relaxation times are derived, together with structural information. The effect of magnetic coupling with another copper ion in Cu2Cu2SOD and Cu2Cu2AP is discussed. It is shown that the electronic relaxation times of copper(II) essentially do not change. The opposite happens with Cu2Co2SOD, Cu2Co2AP and Cu2Ni2SOD in which fast-relaxing metal ions provide relaxation mechanisms for copper(II) as well. In these cases the systems can be studied through high-resolution NMR spectroscopy.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01179525
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    1H NMR investigation of reduced copper-cobalt superoxide dismutase (1991)
    Springer
    European biophysics journal 20 (1991), S. 269-279 
    Details
    ISSN: 1432-1017
    Schlagwort(e): 1HNMR ; Metal substitution ; Superoxide dismutase
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Physik
    Notizen: Abstract Human copper-cobalt superoxide dismutase in the reduced form has been investigated through 1H NMR techniques. The aim is to monitor the structural properties of this derivative and to compare them with those of reduced and oxidized native superoxide dismutases. The observed signals of the cobalt ligands have been assigned as well as the signals of the histidines bound to copper(I). The latter signals experience little pseudocontact shifts which allow a rough orientation of the magnetic susceptibility tensor in the molecular frame. The connectivities indicate that, although the histidine bridge is broken in the reduced form, the interproton distances between ligands of both ions are essentially the same.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00450562
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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