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We introduce a simple theoretical approach for an equilibrium study of\ud   proteins with known native-state structures. We test our approach with\ud   results on well-studied globular proteins, chymotrypsin inhibitor\ud   (2ci2), barnase, and the alpha spectrin SH3 domain, and present evidence\ud   for a hierarchical onset of order on lowering the temperature with\ud   significant organization at the local level even at high temperatures. A\ud   further application to the folding process of HIV-1 protease shows that\ud   the model can be reliably used to identify key folding sites that are\ud   responsible for the development of drug resistance

Conformations of Proteins in Equilibrium