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Diffusional barrier crossing in a two-state protein folding reaction

Nature Structural Biology volume 6, pages 923–926 (1999)Cite this article

Abstract

There has been some debate as to whether protein folding involves diffusive chain motions and thus depends on solvent viscosity. The interpretation of folding kinetics in viscous solvents has remained difficult and controversial, in that viscogenic agents affect folding rates not only by increasing solvent viscosity but also by increasing protein stability. By carefully choosing experimental conditions, we can now eliminate the effect on stability and show that the folding dynamics of the cold shock protein CspB are viscosity dependent. Thus Kramers' theory of reaction rates rather than transition state theory should be used to describe this folding reaction.

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Figure 1: a, Unfolding of CspB in ethylene glycol/water mixtures.
Figure 2: Folding kinetics of CspB.
Figure 3: Viscosity dependence of the folding kinetics of CspB at 54 °C.

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Acknowledgements

We thank Y. Grömping, D. Klostermeier and J. Reinstein for experimental help, and E. Haas, D. Thirumalai, J. Balbach and D. Perl for discussions. This work was supported by by the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie.

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Author notes

  1. Michael Geeves

    Present address: Department of Biosciences, University of Kent, Canterbury, CT2 7NJ, UK

Authors and Affiliations

  1. Laboratorium für Biochemie, Universität Bayreuth, Bayreuth,, D-95440, Germany

    Maik Jacob & Franz X. Schmid

  2. Max-Planck-Institut für molekulare Physiologie, Rheinlanddamm 201, Dortmund, , D-44139, Germany

    Michael Geeves & Georg Holtermann

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  1. Maik Jacob
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  4. Franz X. Schmid
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Correspondence to Franz X. Schmid.

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Jacob, M., Geeves, M., Holtermann, G. et al. Diffusional barrier crossing in a two-state protein folding reaction . Nat Struct Mol Biol 6, 923–926 (1999). https://doi.org/10.1038/13289

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