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.
|Titolo:||Conformations of proteins in equilibrium|
|Autori:||MICHELETTI C; J.R. BANAVAR; A. MARITAN|
|Data di pubblicazione:||2001|
|Digital Object Identifier (DOI):||10.1103/PhysRevLett.87.088102|
|Appare nelle tipologie:||1.1 Journal article|