Journal of Biomolecular NMR

, Volume 10, Issue 2, pp 199–203 | Cite as

Characterisation of protein unfolding by NMR diffusion measurements

  • Jonathan A. Jones
  • Deborah K. Wilkins
  • Lorna J. Smith
  • Christopher M. Dobson


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.

Protein folding Non-native states Hydrodynamic radius Lysozyme 


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Copyright information

© Kluwer Academic Publishers 1997

Authors and Affiliations

  • Jonathan A. Jones
    • 1
  • Deborah K. Wilkins
    • 1
  • Lorna J. Smith
    • 1
  • Christopher M. Dobson
    • 1
  1. 1.Oxford Centre for Molecular Sciences, New Chemistry LaboratoryUniversity of OxfordOxfordU.K

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