𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Mutagenic and Thermodynamic Analyses of Residual Structure in the α Subunit of Tryptophan Synthase†

✍ Scribed by Saab-Rincón, Gloria; Gualfetti, Peter J.; Matthews, C. Robert


Book ID
115491058
Publisher
American Chemical Society
Year
1996
Tongue
English
Weight
498 KB
Volume
35
Category
Article
ISSN
0006-2960

No coin nor oath required. For personal study only.


📜 SIMILAR VOLUMES


Role of conserved proline residues in st
✍ Katsuhide Yutani; Seiko Hayashi; Yoshiko Sugisaki; Kyoko Ogasahara 📂 Article 📅 1991 🏛 John Wiley and Sons 🌐 English ⚖ 789 KB

To study the role of Pro residues in the conformation and conformational stability of a protein, nine mutant alpha subunits of tryptophan synthase from Escherichia coli, in which Ala or Gly was substituted for each of six Pro residues (positions 28, 57, 62, 96, 132, and 207) that are conserved in 10

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