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Hydrodynamic Radii of Native and Denatured Proteins Measured by Pulse Field Gradient NMR Techniques

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Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, England
Cite this: Biochemistry 1999, 38, 50, 16424–16431
Publication Date (Web):November 24, 1999
https://doi.org/10.1021/bi991765q
Copyright © 1999 American Chemical Society

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    Abstract

    Pulse field gradient NMR methods have been used to determine the effective hydrodynamic radii of a range of native and nonnative protein conformations. From these experimental data, empirical relationships between the measured hydrodynamic radius (Rh) and the number of residues in the polypeptide chain (N) have been established; for native folded proteins Rh = 4.75N0.29Å and for highly denatured states Rh = 2.21N0.57Å. Predictions from these equations agree well with experimental data from dynamic light scattering and small-angle X-ray or neutron scattering studies reported in the literature for proteins ranging in size from 58 to 760 amino acid residues. The predicted values of the hydrodynamic radii provide a framework that can be used to analyze the conformational properties of a range of nonnative states of proteins. Several examples are given here to illustrate this approach including data for partially structured molten globule states and for proteins that are unfolded but biologically active under physiological conditions. These reveal evidence for significant coupling between local and global features of the conformational ensembles adopted in such states. In particular, the effective dimensions of the polypeptide chain are found to depend significantly on the level of persistence of regions of secondary structure or features such as hydrophobic clusters within a conformational ensemble.

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     This is a contribution from the Oxford Centre for Molecular Sciences, which is supported by the U.K. Engineering and Physical Sciences Research Council, the Biotechnology and Biological Sciences Research Council, and the Medical Research Council. The research of C.M.D. is supported in part by the Wellcome Trust and by an International Research Scholars award from the Howard Hughes Medical Research Institute. L.J.S. and J.A.J. are Royal Society University Research Fellows. V.R. was supported by an EMBO fellowship.

     Present address:  AFMB−CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille, France.

    §

     Present address:  Clarendon Laboratory, University of Oxford, Parks Road, Oxford OX1 3PU, England.

    *

     Corresponding author:  Phone:  +44−1865−275961; FAX +44−1865−275921; E-mail [email protected].

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    Three tables listing hydrodynamic radii and radii of gyration data taken from the literature that were used in the analysis presented in this paper. The material is available free of charge via the Internet at http://pubs.acs.org.

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