Optical measurement of a solvent-induced isomerization in a proline-containing hexapeptide
- 1 July 1979
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 89 (2) , 591-597
- https://doi.org/10.1016/0006-291x(79)90671-5
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease AJournal of Molecular Biology, 1978
- Cis‐Trans equilibrium and kinetic studies of acetyl‐L‐proline and glycyl‐L‐prolineBiopolymers, 1977
- PK Changes of Ionizable Reporter Groups as an Index of Conformational Changes in Proteins. A Study of Fluorescein-Labelled Ribonuclease AEuropean Journal of Biochemistry, 1976
- The X‐Pro peptide bond as an nmr probe for conformational studies of flexible linear peptidesBiopolymers, 1976
- Nmr studies of the molecular conformations in the linear oligopeptides H-(L-Ala)n-L-Pro-OHBiopolymers, 1976
- Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residuesBiochemistry, 1975
- A physical difference between the fast- and slow-refolding forms of nitrotyrosyl ribonuclease A: the pK values of the nitrotyrosyl groupsJournal of Molecular Biology, 1975
- Nuclear magnetic resonance studies of the acid-base chemistry of amino acids and peptides. II. Dependence of the acidity of the C-terminal carboxyl group on the conformation of the C-terminal peptide bondJournal of the American Chemical Society, 1974
- A novel approach for studies of the molecular conformations in flexible polypeptidesFEBS Letters, 1974
- Tetranitromethane. A Reagent for the Nitration of Tyrosyl Residues in Proteins*Biochemistry, 1966