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
✦ LIBER ✦
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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