Redox-Triggered Secondary Structure Changes in the Aggregated States of a Designed Methionine-Rich Peptide
Author:
Affiliation:
1. Contribution from the Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja962026p
Reference42 articles.
1. Dominant forces in protein folding
2. Redox control of secondary structure in a designed peptide
3. Comparing the polarities of the amino acids: side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution
4. Oxidation of methionyl residues in proteins: Tools, targets, and reversal
5. Disruption of coiled coil formation by methionine oxidation
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