Simulation of the activation of alpha-chymotrypsin: analysis of the pathway and role of the propeptide.

ABSTRACT: Alpha-chymotrypsin undergoes a reversible conformational change from an inactive chymotrypsinogen-like structure at high pH to an active conformation at neutral pH. In order to gain insight into this process on a structural level, we applied molecular dynamics and targeted molecular dynamics simulations in aqueous environment on the activation and inactivation processes of three different types of chymotrypsin. These are the wild-type bovine chymotrypsin containing the propeptide and the bovine and rat chymotrypsin lacking the propeptide. From these simulations, the importance of the propeptide and of the sequence differences between the rat and bovine variants from the viewpoint of activation could be evaluated and compared with previous fluorescence stopped flow results. The obtained res

SUBMITTER: Matrai J 

PROVIDER: S-EPMC2287318 | biostudies-literature | 2004 Dec

REPOSITORIES: biostudies-literature