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Characterization of the slow steps in the folding of the .alpha. subunit of tryptophan synthase

โœ Scribed by Crisanti, Mark M.; Matthews, C. Robert


Book ID
126067384
Publisher
American Chemical Society
Year
1981
Tongue
English
Weight
888 KB
Volume
20
Category
Article
ISSN
0006-2960

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๐Ÿ“œ SIMILAR VOLUMES


Characterization of a slow folding react
โœ Mark R. Hurle; Greg A. Michelotti; Mark M. Crisanti; Dr. C. Robert Matthews ๐Ÿ“‚ Article ๐Ÿ“… 1987 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 850 KB

The equilibria and kinetics of urea-induced unfolding and refolding of the alpha subunit of tryptophan synthase of E. coli have been examined for their dependences on viscosity, pH, and temperature in order to investigate the properties of one of the rate-limiting steps, domain association. A viscos

Kinetic characterization of early interm
โœ Sylvie Blond; Dr. Michel E. Goldberg ๐Ÿ“‚ Article ๐Ÿ“… 1986 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 841 KB

This report describes the use of fluorescence energy transfer between an intrinsic energy donor (tryptophan 177) and two chemically added acceptors to study intermediates in the folding of the beta 2 subunit of E. coli tryptophan-synthase. Two early folding steps are thus identified and characterize