Proline cis-trans isomerization and protein folding

Détails

ID Serval
serval:BIB_93A3B7FECE3D
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Proline cis-trans isomerization and protein folding
Périodique
Biochemistry
Auteur(s)
Wedemeyer  W. J., Welker  E., Scheraga  H. A.
ISSN
0006-2960 (Print)
Statut éditorial
Publié
Date de publication
12/2002
Volume
41
Numéro
50
Pages
14637-44
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: Dec 17
Résumé
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.
Mots-clé
Animals Cattle Isoenzymes/chemistry Models, Chemical Proline/*chemistry Protein Conformation *Protein Folding Ribonuclease, Pancreatic/chemistry Stereoisomerism
Pubmed
Web of science
Création de la notice
24/01/2008 15:40
Dernière modification de la notice
03/03/2018 19:35
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