Thermodynamic Properties of the Transition State for the Rate-Limiting Step in the Folding of the .alpha. Subunit of Tryptophan Synthase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00186a040
Reference50 articles.
1. Characterization of an early intermediate in the folding of the .alpha. subunit of tryptophan synthase by hydrogen exchange measurement
2. Effects of the phenylalanine-22 .fwdarw. leucine, glutamic acid-49 .fwdarw. methionine, glycine-234 .fwdarw. aspartic acid and glycine-234 .fwdarw. lysine mutations on the folding and stability of the .alpha. subunit of tryptophan synthase from Escherichia coli
3. Protein stability curves
4. Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
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