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Published November 1998 | public
Journal Article

Protein Folding Triggered by Electron Transfer

Abstract

Proteins do not fold by randomly searching a large number of nearly degenerate configurations; instead, an ensemble of unfolded molecules must traverse a complicated energy landscape to reach a thermodynamically stable structure. The fastest nuclear motions in proteins, rotations about single bonds, occur on the picosecond time scale and accompany both secondary- and tertiary-structure-forming processes. Short segments of secondary structure (e.g., α-helices) can be formed in nanoseconds, whereas the large-scale, collective motions associated with the development of tertiary structure fall in the microsecond to millisecond range. Misfolded structures or traps are frequently encountered in folding processes; escape from these traps (e.g., proline isomerization) can take seconds or even minutes. Understanding the key events in folding and identifying any partially folded intermediates are major goals of theoretical and experimental work.

Additional Information

© 1998 American Chemical Society. Received January 16, 1998. Publication Date (Web): October 28, 1998. This work was supported by the NSF (Grant MCB-9630465 to J.R.W.; Grant CHE-9508533 to H.B.G.). Postdoctoral fellowships from the NIH (J.R.T.) and TFR-Sweden (P.W.-S.) are acknowledged with thanks. Important contributions to our ET-triggered folding studies have been made by Gary Mines, John Chesick, Sonny Lee, Don Low, Bo Malmström, Torbjörn Pascher, and F. Akif Tezcan. We also thank Bill Eaton, George McLendon, José Onuchic, and Peter Wolynes for helpful discussions. H.B.G. thanks Balliol College and the Inorganic Chemistry Laboratory, University of Oxford, for providing a stimulating intellectual environment during 1997−98.

Additional details

Created:
August 19, 2023
Modified:
October 17, 2023