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  • Hydrodynamic radius  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of biomolecular NMR 10 (1997), S. 199-203 
    ISSN: 1573-5001
    Keywords: Protein folding ; Non-native states ; Hydrodynamic radius ; Lysozyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The characterisation of non-native states of proteins is a key problem instudies of protein folding. Complete characterisation of these states requiresa description of both local and global properties, including moleculardimensions. Here we present results from pulsed field gradient experimentsdesigned to compare the effective hydrodynamic radii of a protein in nativeand non-native states. Measurements performed on lysozyme indicate that theeffective hydrodynamic radius increases by 38±1% on unfolding in urea,a result completely consistent with a recent study by small-angle X-rayscattering.
    Type of Medium: Electronic Resource
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