Conformational changes of alpha-chymotrypsin in a fibrillation-promoting condition: a molecular dynamics study.

ABSTRACT: Amyloid nanofibril formation appears to be a generic property of polypeptide chains. alpha-Chymotrypsin (aCT) was recently driven toward amyloid-like aggregation by the addition of trifluoroethanol (TFE) at intermediate concentrations. In this study we employed a molecular dynamics simulation to investigate the early events in TFE-induced conformational changes of aCT that precede amyloid formation, and compared the results of the simulation with previous experiments. TFE molecules were found to rapidly replace the water molecules closely associated with the protein surface. The gyration radius, together with total and hydrophobic solvent-accessible surface areas of aCT, was significantly increased. In accord with the experimental observations, the extended beta-conformation of backbone wa

SUBMITTER: Rezaei-Ghaleh N 

PROVIDER: S-EPMC2567952 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature