Snapshots of cytochrome c folding

Creators: Pletneva, Ekaterina V.; Gray, Harry B.; Winkler, Jay R.

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Abstract

Dansyl-to-heme distance distributions [P(r)] during folding have been determined in five variants of Saccharomyces cerevisiae iso-1 ferricytochrome c (labeled at mutant Cys residues 4, 39, 50, 66, and 99) by analysis of fluorescence energy-transfer kinetics. Moment analysis of the P(r) distributions clearly indicates that cytochrome c refolding is not a simple two-state process. After 1 ms of folding, the polypeptide ensemble is not uniformly collapsed and there are site variations in the relative populations of collapsed structures. P(r) distributions reveal structural features of the multiple intermediate species and evolution of the polypeptide ensemble.

Additional Information

© 2005 by the National Academy of Sciences Contributed by Harry B. Gray, October 17, 2005 We acknowledge Yuling Sheng for her help with protein expression and purification during the final stages of this work. We also thank Jennifer C. Lee and Judy E. Kim for help with FET kinetics measurements and numerous discussions. This work was supported by National Institutes of Health Grant GM068461 (to J.R.W.) and an Ellison Medical Foundation Senior Scholar Award in Aging (to H.B.G.). Author contributions: E.V.P., H.B.G., and J.R.W. designed research; E.V.P. performed research; E.V.P. and J.R.W. analyzed data; and E.V.P., H.B.G., and J.R.W. wrote the paper. Conflict of interest statement: No conflicts declared.

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