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