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Protein folding triggered by electron transfer
Author(s): Pascher T, Chesick JP, Winkler JR, Gray HB
Source: SCIENCE    Volume: 271    Issue: 5255    Pages: 1558-1560    Published: MAR 15 1996  
Times Cited: 245     References: 32     
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 degrees 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.
Document Type: Article
Language: English
Addresses:
1. CALTECH, BECKMAN INST, PASADENA, CA 91125 USA
2. HAVERFORD COLL, HAVERFORD, PA 19041 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005
Subject Category: Multidisciplinary Sciences
IDS Number: TZ983
ISSN: 0036-8075
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