title: Proline cis-trans isomerization and protein folding.
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.
authors.affiliation: Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301, USA.
authors.forename: William J
authors.initials: WJ
authors.lastname: Wedemeyer
authors.forename: Ervin
authors.initials: E
authors.lastname: Welker
authors.forename: Harold A
authors.initials: HA
authors.lastname: Scheraga
mesh_terms: D000818:Animals; D002417:Cattle; D007527:Isoenzymes / Q000737:chemistry; D008956:Models, Chemical; D011392:Proline / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D013237:Stereoisomerism
chemical_list: D007527:Isoenzymes; D011392:Proline; D012259:Ribonuclease, Pancreatic