| Literature DB >> 12475212 |
William J Wedemeyer1, Ervin Welker, Harold A Scheraga.
Abstract
Proline cis-trans isomerization plays a key role in the rate-determining steps of protein folding. The energetic origin of this isomerization process is summarized, and the folding and unfolding of disulfide-intact bovine pancreatic ribonuclease A is used as an example to illustrate the kinetics and structural features of conformational changes from the heterogeneous unfolded state (consisting of cis and trans isomers of X-Pro peptide groups) to the native structure in which only one set of proline isomers is present.Entities:
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Year: 2002 PMID： 12475212 DOI： 10.1021/bi020574b
Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162