Conformations of proteins in equilibrium.
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.
Micheletti
C
C
International School for Advanced Studies (S.I.S.S.A.) and INFM, Via Beirut 2-4, 34014 Trieste, Italy.
Banavar
J R
JR
Maritan
A
A
D000818:Animals; D001426:Bacterial Proteins; D055592:Biophysical Phenomena; D001703:Biophysics; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D016333:HIV Protease / Q000737:chemistry; D006801:Humans; D066298:In Vitro Techniques; D008956:Models, Chemical; D010455:Peptides; D010940:Plant Proteins / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D012260:Ribonucleases / Q000737:chemistry; D013049:Spectrin / Q000737:chemistry; D013816:Thermodynamics
D001426:Bacterial Proteins; D010455:Peptides; D010940:Plant Proteins; D011506:Proteins; C093336:chymotrypsin inhibitor 2; D013049:Spectrin; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease; D016333:HIV Protease