Ten-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase·PhCH_20~- complex

摘要

Molecular dynamics simulations have been carried out for a period of 10 ns with the dimeric enzyme horse liver alcohol dehydroge-nase (HLADH) present as the reactive complex HLADH·NAD~+·PhCH_2O~-. Cross-correlation analysis of the trajectory was carried out with the latter from 500 ps to 10 ns. The resulting cross-correlation map allowed the identification of the correlated and anticorrelated motions, which involve the entire protein. Anticor-related and correlated motions are carried into the active site-aligned residues.