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Hierarchical folding of cytochrome c

Nature Structural Biology volume 7, pages 443–445 (2000)Cite this article

Formation of secondary structure during protein folding can now be probed on the submillisecond time scale. By monitoring the formation of α-helix formation during the initial collapse of cytochrome c, its folding mechanism is delineated.

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Acknowledgements

We thank E. Stellwagen of the University of Iowa for helpful discussions. This work was supported by a grant from the National Institutes of Health.

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Authors and Affiliations

  1. the Department of Physiology and Biophysics, Albert Einstein College of Medicine, Yeshiva University, Resnick Campus, 1300 Morris Park Avenue, Bronx, 10461, New York, USA

    Syun-Ru Yeh & Denis L. Rousseau

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  1. Syun-Ru Yeh
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  2. Denis L. Rousseau
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Correspondence to Denis L. Rousseau.

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Yeh, SR., Rousseau, D. Hierarchical folding of cytochrome c. Nat Struct Mol Biol 7, 443–445 (2000). https://doi.org/10.1038/75831

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