Folding/unfolding kinetics of mutant forms of iso-1-cytochrome c with replacement of proline-71
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00370a033
Reference44 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. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
4. Empirical Predictions of Protein Conformation
5. Characterization of the slow steps in the folding of the .alpha. subunit of tryptophan synthase
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1. The role of key residues in structure, function, and stability of cytochrome-c;Cellular and Molecular Life Sciences;2013-04-25
2. Time-Resolved Mass Spectrometry for Monitoring Millisecond Time-Scale Solution-Phase Processes;European Journal of Mass Spectrometry;2012-04
3. Stabilization of Partially Folded States of Cytochrome C in Aqueous Surfactant: Effects of Ionic and Hydrophobic Interactions;Biochemistry;2003-11-20
4. Multiple roles of prolyl residues in structure and folding 1 1Edited by C. Robert Matthews;Journal of Molecular Biology;2000-08
5. Chapter 5 Protein folding;Protein Volume 2;1999
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