[26] Effect of point mutations of the folding of globular proteins
- 1 January 1987
- book chapter
- Published by Elsevier
- Vol. 154, 498-511
- https://doi.org/10.1016/0076-6879(87)54092-7
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- 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 coliBiochemistry, 1986
- Effects of guanidine hydrochloride on the refolding kinetics of denatured thioredoxinBiochemistry, 1986
- Conformational stability of mixed disulfide derivatives of .beta.-lactoglobulin BBiochemistry, 1983
- Effect of a single amino acid substitution on the folding of the .alpha. subunit of tryptophan synthaseBiochemistry, 1983
- Guanidine hydrochloride-induced unfolding of the .alpha. subunit of tryptophan synthase and of the two .alpha. proteolytic fragments: evidence for stepwise unfolding of the two .alpha. domainsBiochemistry, 1982
- Characterization of the slow steps in the folding of the .alpha. subunit of tryptophan synthaseBiochemistry, 1981
- Solvent denaturationBiopolymers, 1978
- A quantitative treatment of the kinetics of the folding transition of ribonuclease ABiochemistry, 1976
- The Stability of Globular ProteinCRC Critical Reviews in Biochemistry, 1975
- Principles that Govern the Folding of Protein ChainsScience, 1973