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The burst phase in ribonuclease A folding and solvent dependence of the unfolded state

Nature Structural Biology volume 5, pages 882–884 (1998)Cite this article

Abstract

Submillisecond burst phase signals measured in kinetic protein folding experiments have been widely interpreted in terms of the fast formation of productive folding intermediates. Experimental comparisons with non-folding polypeptide chains show that, for ribonuclease A and cytochrome c , these signals in fact reflect a shift from one biased ensemble of the unfolded state to another as a function of change in denaturant concentration.

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Figure 1: Melting behavior of native RNase A (closed circles) and the disulfide-broken polypeptide (open triangles).
Figure 2: Kinetic traces of refolding by stopped-flow CD.
Figure 3: Dependence of kinetic amplitudes on final GmCl concentration.

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Acknowledgements

This work was supported by NIH research grants to S.W.E. and T.R.S.

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Authors and Affiliations

  1. Department of Biochemistry and Biophysics, The Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, 19104-6059, Pennsylvania, USA

    Phoebe X. Qi & S. Walter Englander

  2. Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, 60637-1432, Illinois, USA

    Tobin R. Sosnick

Authors
  1. Phoebe X. Qi
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  2. Tobin R. Sosnick
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Correspondence to Phoebe X. Qi.

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Qi, P., Sosnick, T. & Englander, S. The burst phase in ribonuclease A folding and solvent dependence of the unfolded state . Nat Struct Mol Biol 5, 882–884 (1998). https://doi.org/10.1038/2321

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