Ten-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase⋅PhCH(2)O(−) complex

Molecular dynamics simulations have been carried out for a period of 10 ns with the dimeric enzyme horse liver alcohol dehydrogenase (HLADH) present as the reactive complex HLADH⋅NAD(+)⋅ PhCH(2)O(−). 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. Anticorrelated and correlated motions are carried into the active site-aligned residues.