Article
Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction.
Biochemistry - 13 Feb 1990
Tweedy N B, Hurle M R, Chrunyk B A, Matthews C R
Abstract excerpt
Equilibrium and kinetic studies on the folding of a series of amino acid replacements at position 211 in the alpha subunit of tryptophan synthase from Escherichia coli were performed in order to determine the role of this position in the rate-limiting step in folding. Previous studies [Beasty, A. M., Hurle, M. R., Manz, J. T., Stackhouse, T., Onuffer, J. J., & Matthews, C. R. (1986) Biochemistry 25, 2965-2974]...
Topics
- Amino Acids
- Chemical Phenomena
- Chemistry
- Escherichia coli
- Hydrogen Bonding
- Kinetics
- Mutation
- Protein Conformation
- Thermodynamics
- Tryptophan Synthase
- Urea
