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Biophysics

Rough passage across a barrier

Nature volume 502, pages 632–633 (2013)Cite this article

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The dynamics of chemical reactions in solution are described by Kramers' theory, but the parameters involved have eluded direct measurement. A study of protein folding reveals how this problem can be overcome. See Letter p.685

Proteins fluctuate between different conformations to perform their sophisticated tasks. The random motion of water molecules around proteins provides an inexhaustible reservoir of thermal 'kicks', which act as the molecular driving forces of such conformational dynamics. Counter-intuitively, the same thermal motions of the solvent also limit the speed of biomolecular motion, an effect known as solvent friction. But it has become increasingly clear that, in some important cases, friction within a protein molecule might be the dominant impediment to its molecular dynamics. In this issue, Chung and Eaton1 (page 685) report one of the most impressive studies so far in which the contribution of such internal friction to dynamics is quantified for protein molecules caught in the act of folding. Remarkably, the results have implications far beyond protein foldingFootnote 1.

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Figure 1: Barrier crossing in protein folding.

Notes

  1. *This article and the paper under discussion1 were published online on 23 October 2013.

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Authors and Affiliations

  1. Benjamin Schuler is in the Department of Biochemistry, University of Zurich, 8057 Zurich, Switzerland.,

    Benjamin Schuler

  2. Jane Clarke is a Wellcome Trust Senior Research Fellow in the Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.,

    Jane Clarke

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  1. Benjamin Schuler
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  2. Jane Clarke
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Correspondence to Benjamin Schuler or Jane Clarke.

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Schuler, B., Clarke, J. Rough passage across a barrier. Nature 502, 632–633 (2013). https://doi.org/10.1038/nature12697

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