Journal
BIOCHEMISTRY
Volume 41, Issue 50, Pages 14637-14644Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi020574b
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- NIGMS NIH HHS [GM-24893] Funding Source: Medline
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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.
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