Cis-Trans Imide Isomerization of the Proline Dipeptide
- 1 December 1994
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 116 (26) , 11931-11937
- https://doi.org/10.1021/ja00105a036
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- Occurrence and role ofcis peptide bonds in protein structuresPublished by Elsevier ,2005
- The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen.Journal of Biological Chemistry, 1987
- Dynamical theory of activated processes in globular proteins.Proceedings of the National Academy of Sciences, 1982
- The rate of interconversion between the two unfolded forms of ribonuclease A does not depend on guanidinium chloride concentrationJournal of Molecular Biology, 1979
- Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerizationProceedings of the National Academy of Sciences, 1978
- Theoretical studies of environmental effects on protein conformation. 1. Flexibility of the peptide bondJournal of the American Chemical Society, 1977
- Cis‐Trans equilibrium and kinetic studies of acetyl‐L‐proline and glycyl‐L‐prolineBiopolymers, 1977
- Determination of the rates and barriers to conformational isomerization in the dipeptide L‐pro‐L‐4hyp by direct 13C nmr thermal equilibrationBiopolymers, 1977