Ontology highlight
ABSTRACT:
SUBMITTER: Montalvo G
PROVIDER: S-EPMC2862463 | biostudies-literature | 2010 Apr
REPOSITORIES: biostudies-literature
Montalvo Geronda G Waegele Matthias M MM Shandler Scott S Gai Feng F DeGrado William F WF
Journal of the American Chemical Society 20100401 16
Synthetic foldamers consisting of beta-amino acids offer excellent model systems for examining the effect of backbone flexibility on the dynamics of protein folding. Herein, we study the folding-unfolding kinetics of a beta-peptide that folds into a 14-helical structure in water. We find that the T-jump induced relaxation kinetics of this peptide occur on the nanosecond time scale and are noticeably slower than those of alanine-based alpha-helical peptides, and additionally, the relaxation rates ...[more]