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Spectroscopic Studies of Ferrocytochrome c Folding

Mines, Gary A. and Winkler, Jay R. and Gray, Harry B. (1998) Spectroscopic Studies of Ferrocytochrome c Folding. In: Spectroscopic Methods in Bioinorganic Chemistry. ACS Symposium Series. No.692. American Chemical Society , Washington, DC, pp. 198-211. ISBN 9780841235601.

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Electron-transfer triggering has been employed in a comparison of the folding energetics and kinetics of cytochrome c from horse and Saccharomyces cerevisiae. These two proteins, with just 60% sequence identity but very similar backbone structures, fold at very different rates at a given denaturant concentration, but at nearly the same rate when their folding free energies are the same. Differences in the amino-acid sequences shift the position of the folding/unfolding equilibrium, but do not appear to alter the location of the transition state along the folding coordinate.

Item Type:Book Section
Related URLs:
URLURL TypeDescription
Winkler, Jay R.0000-0002-4453-9716
Gray, Harry B.0000-0002-7937-7876
Additional Information:© 1998 American Chemical Society. Published in print 9 June 1998. This work was supported by the National Science Foundation (MCB-9630465), the National Institutes of Health, and the Arnold and Mabel Beckman Foundation.
Funding AgencyGrant Number
Arnold and Mabel Beckman FoundationUNSPECIFIED
Series Name:ACS Symposium Series
Issue or Number:692
Record Number:CaltechAUTHORS:20180406-091535617
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Official Citation:Spectroscopic Studies of Ferrocytochrome c Folding Gary A. Mines, Jay R. Winkler, and Harry B. Gray Spectroscopic Methods in Bioinorganic Chemistry. June 9, 1998, 198-211 DOI:10.1021/bk-1998-0692.ch010
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:85677
Deposited By: Ruth Sustaita
Deposited On:06 Apr 2018 17:42
Last Modified:15 Nov 2021 20:31

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