Proline cis-trans isomerization and protein folding.
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.
Wedemeyer
William J
WJ
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301, USA.
Welker
Ervin
E
Scheraga
Harold A
HA
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
D007527:Isoenzymes; D011392:Proline; D012259:Ribonuclease, Pancreatic