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  • Electric quadrupole interaction  (1)
  • relaxation  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Perturbed angular correlation studies of the metal-binding sites in ovotransferrin and its C- and N-terminal halves (1993)
    Springer
    BioMetals 6 (1993), S. 193-201 
    Details
    ISSN: 1572-8773
    Keywords: electric quadrupole interaction ; 181Hf ; ovotransferrin ; perturbed angular correlations ; relaxation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The perturbed angular correlation (PAC) technique has been applied to study the electric quadrupole interaction of 181Hf nuclei at the binding sites of ovotransferrin (OTF) molecules. Two specific electric field gradients were observed. Their relative intensities depend on the pH value and the temperature of the samples, whereas the electric quadrupole interaction parameters themselves remain unaffected. In order to compare the binding sites in OTF, experiments with N- and C-terminal half-molecules were performed. Both specific configurations are observed at the N-terminal and at the C-terminal binding site with similar quadrupole parameters as for the intact protein. Remarkably, the stability of the hafnium binding to the C-terminal fragment appears to be reduced as compared with the N-terminal half and the intact protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00205859
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Influence of protein dynamics on the metal-sites of ovotransferrin (1992)
    Springer
    European biophysics journal 21 (1992), S. 147-154 
    Details
    ISSN: 1432-1017
    Keywords: Ovotransferrin ; Protein dynamics ; Time differential perturbed angular correlations ; Electric quadrupole interaction ; Relaxation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Using the perturbed angular correlations (PAC) technique, the formation of hafnium-ovotransferrin complexes has been studied. Two binding configurations at each of the two specific binding-sites of the protein have been observed. They are characterized by well-defined electric quadrupole frequencies. Information about the dynamics of the protein was derived from temperature dependent measurements of the relaxation constant. The well-resolved spectra taken with fast BaF2-detectors allow a precise determination of the relaxation behaviour of the protein. The results are compared with the predictions from a hydrodynamic model for the reorientation of macromolecules. Thus the hydrodynamic volume of ovotransferrin and its N-terminal half-molecule were determined. The ovotransferrin volume is in agreement with a value derived for human serum transferrin from small angle neutron scattering. From experiments with immobilized protein material there is evidence for internal protein dynamics which is probed by the Hf-ion bound to the specific metal-sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00185429
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    Paper (German National Licenses)
    Fulltext
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