Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate.

ABSTRACT: The acylation mechanism of a prototypical serine protease trypsin and its complete free energy reaction profile have been determined by Born-Oppenheimer ab initio QM/MM molecular dynamics simulations with umbrella sampling.

SUBMITTER: Zhou Y 

PROVIDER: S-EPMC3213857 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature