Conformations of proteins in equilibrium - art. no. 088102

We introduce a simple theoretical approach for an equilibrium study of prot eins 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 fo lding process of HIV-1 protease shows that the model can be reliably used t o identify key folding sites that are responsible for the development of dr ug resistance.