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NMR evidence for the stepwise unfolding of the two domains of tryptophan synthase α-subunit

✍ Scribed by Hideo Iwahashi; Katsuhide Yutani; Kyoko Ogasahara; Susumu Tsunasawa; Yoshimasa Kyogoku; Yoshinobu Sugino


Book ID
113264147
Publisher
Elsevier Science
Year
1983
Tongue
English
Weight
257 KB
Volume
744
Category
Article
ISSN
0167-4838

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✍ 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