Conformations of Proteins in Equilibrium

Details Conformations of Proteins in Equilibrium Conformations of Proteins in Equilibrium

2001-07-31

arxiv.org/abs/cond-mat/0107624v1

Physics

Condensed Matter

Statistical Mechanics

6 pages, 3 eps figures

Scientific paper

10.1103/PhysRevLett.87.088102

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 .

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