Correlation of Folding Kinetics with the Number and Isomerization States of Prolines in Three Homologous Proteins of the Rnase Family.
From: Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA.
FEBS letters
- Publish Date: Sep 2006
- ISSN: 0014-5793
- Volume: 580
- Issue: 21
- Pages: 5029-32
- Medium: Print
- Language: English
- Citation (JAMA): Pradeep Lovy, Shin Hang-Cheol, Scheraga Harold A, et al. Correlation of Folding Kinetics with the Number and Isomerization States of Prolines in Three Homologous Proteins of the Rnase Family.. FEBS Lett. Sep 2006;580:5029-32
Abstract
Several studies attribute the slower phases in protein folding to prolyl isomerizations, and several others do not. A correlation exists between the number of prolines in a protein and the complexity of the mechanism with which it folds. In this study, we have demonstrated a direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds via slower phases by studying the folding of three structurally homologous proteins of the ribonuclease family, namely RNase A, onconase and angiogenin, which differ in the number and isomerization states of their proline residues.
Mesh Headings (Keywords): Animals, Anura, Cattle, Kinetics, Proline, Protein Folding, Protein Structure, Secondary, Ribonuclease, Pancreatic, Ribonucleases, Stereoisomerism
Check for Full Text / PubMed Unique Identifier (PMID): 16949585
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.