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The progressive development of structure and stability during the equilibrium folding of the α subunit of tryptophan synthase from Escherichia coli

✍ Scribed by Peter J. Gualfetti; Osman Bilsel; C. Robert Matthews


Book ID
111753670
Publisher
Cold Spring Harbor Laboratory Press
Year
1999
Tongue
English
Weight
1014 KB
Volume
8
Category
Article
ISSN
0961-8368

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📜 SIMILAR VOLUMES


Characterization of a slow folding react
✍ Mark R. Hurle; Greg A. Michelotti; Mark M. Crisanti; Dr. C. Robert Matthews 📂 Article 📅 1987 🏛 John Wiley and Sons 🌐 English ⚖ 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
✍ Sylvie Blond; Dr. Michel E. Goldberg 📂 Article 📅 1986 🏛 John Wiley and Sons 🌐 English ⚖ 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