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 .