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Published March 15, 1996 | public
Journal Article

Protein Folding Triggered by Electron Transfer

Abstract

Rapid photochemical electron injection into unfolded ferricytochrome c titrated with 2.3 to 4.6 M guanidine hydrochloride (GuHCl) at pH 7 and 40°C produced unfolded ferrocytochrome, which then converted to the folded protein. Two folding phases were observed: a fast process with a time constant of 40 microseconds (4.6 M GuHCl), and a slower phase with a rate constant of 90 ± 20 per second (2.3 M GuHCl). The activation free energy for the slow step varied linearly with GuHCl concentration; the rate constant, extrapolated to aqueous solution, was 7600 per second. Electron-transfer methods can bridge the nanosecond to millisecond measurement time gap for protein folding.

Additional Information

© 1996 American Association for the Advancement of Science. 5 December 1995; Accepted 29 January 1996. We thank G. Mines and S. Lee for technical assistance, M. Gruebele for a preprint of his paper on apomyoglobin, and P. Wolynes for helpful discussions. Supported by the Swedish Natural Science Research Council (T.P.), NIH, NSF, and the Arnold and Mabel Beckman Foundation.

Additional details

Created:
August 20, 2023
Modified:
October 19, 2023