Wittung-Stafshede, Pernilla and Lee, Jennifer C. and Winkler, Jay R. and Gray, Harry B. (1999) Cytochrome b562 folding triggered by electron transfer: Approaching the speed limit for formation of a four-helix-bundle protein. Proceedings of the National Academy of Sciences of the United States of America, 96 (12). pp. 6587-6590. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:WITpnas99
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Ferrocytochrome b(562) [Fe(II)cyt b(562)] folding can be triggered by photoinduced electron transfer to unfolded Fe (III)cyt b(562) in 2-3 M guanidine hydrochloride solutions. The folding rates increase with decreasing guanidine hydrochloride; the extrapolated time constant for this folding process in the absence of denaturant (5 mu s) is near the predicted value for intrachain diffusion. The relatively smooth energy landscape indicated for Fe(II)cyt b(562) folding accords with the helical, highly symmetrical structure of the protein.
|Additional Information:||Copyright © 1999 by the National Academy of Sciences. Contributed by Harry B. Gray, April 6, 1999. We thank Kevin Plaxco and Peter Wolynes for communication of unpublished results as well as several stimulating discussions. P.W.-S. acknowledges a postdoctoral fellowship from the Swedish Technical Research Council. J.C.L. acknowledges a graduate fellowship from the Ralph M. Parsons Foundation. This work was supported by the National Science Foundation (Grant MCB 9630465). The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.|
|Subject Keywords:||protein folding, guanidine hydrochloride, contact order, A binding-protein, 4-helix bundle, Escherichia-coli, kinetics, thermodynamics, perspective, mechanism, dynamics, events|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||15 Nov 2005|
|Last Modified:||14 Nov 2014 19:18|
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