Redox-Triggered Secondary Structure Changes in the Aggregated States of a Designed Methionine-Rich Peptide
- 1 January 1996
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 118 (50) , 12487-12494
- https://doi.org/10.1021/ja962026p
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Disruption of coiled coil formation by methionine oxidationBioorganic & Medicinal Chemistry Letters, 1996
- Cooperatively folded proteins in random sequence librariesNature Structural & Molecular Biology, 1995
- Oxidation of methionyl residues in proteins: Tools, targets, and reversalFree Radical Biology & Medicine, 1995
- Analytical Ultracentrifugation of Complex Macromolecular SystemsBiochemistry, 1994
- Redox control of secondary structure in a designed peptideJournal of the American Chemical Society, 1993
- A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper MutantsScience, 1993
- Synthetic approaches to biologically active peptides and proteins including enzymesAccounts of Chemical Research, 1989
- Comparing the polarities of the amino acids: side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solutionBiochemistry, 1988
- Induction of peptide conformation at apolar water interfaces. 1. A study with model peptides of defined hydrophobic periodicityJournal of the American Chemical Society, 1985
- Computed circular dichroism spectra for the evaluation of protein conformationBiochemistry, 1969