Phys. Rev. Lett., 87, DOI:088102-1 (2001)

Conformations of proteins in equilibrium

C. Micheletti, J.R. Banavar and A. Maritan

Link to online article. ABSTRACT. 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 .