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Identifying the structural boundaries of independent folding domains in the a subunit of tryptophan synthase, a β/α barrel protein

✍ Scribed by Jill A. Zitzewitz; Peter J. Gualfetti; Ieva A. Perkons; Stacey A. Wasta; C. Robert Matthews


Book ID
111753637
Publisher
Cold Spring Harbor Laboratory Press
Year
1999
Tongue
English
Weight
625 KB
Volume
8
Category
Article
ISSN
0961-8368

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Roles for the two N-terminal (β/α) modul
✍ Satoshi Akanuma; Akihiko Yamagishi 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 430 KB

## Abstract The (β/α)~8~‐barrel is one of the most abundant folds found in enzymes. To identify the independent folding units and the segment(s) that correspond to a minimum core structure within a (β/α)~8~‐barrel protein, fragmentation experiments were performed with __Escherichia coli__ phosphori