Kinetics and importance of the dimerization step in the folding pathway of the β2 subunit of Escherichia coli tryptophan synthase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference28 articles.
1. Assignment of the ends of the β-chain of E. coli tryptophan synthase to the F1 and F2 domains
2. Experimental studies of protein folding and unfolding
3. Kinetic studies of tryptophan synthetase. Interaction of substrates with the B subunit
4. Relationship between the activity of the 3 beta-hydroxysteroid dehydrogenase from bovine adrenal cortex microsomes and membrane structure. Influence of proteins and steroid substrates on lipid “microviscosity”.
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