Conformations of Proteins in Equilibrium
Journal Article
·
· Physical Review Letters
We introduce a simple theoretical approach for an equilibrium study of proteins with known native-state structures. We test our approach with results on well-studied globular proteins, chymotrypsin inhibitor (2ci2), barnase, and the alpha spectrin SH3 domain, and present evidence for a hierarchical onset of order on lowering the temperature with significant organization at the local level even at high temperatures. A further application to the folding process of HIV-1 protease shows that the model can be reliably used to identify key folding sites that are responsible for the development of drug resistance.
- Sponsoring Organization:
- (US)
- OSTI ID:
- 40231012
- Journal Information:
- Physical Review Letters, Vol. 87, Issue 8; Other Information: DOI: 10.1103/PhysRevLett.87.088102; Othernumber: PRLTAO000087000008088102000001; 028134PRL; PBD: 20 Aug 2001; ISSN 0031-9007
- Publisher:
- The American Physical Society
- Country of Publication:
- United States
- Language:
- English
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