Ten-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase.PhCH2O- 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+. PhCH2O-. 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.
Luo
Jia
J
Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, USA.
Bruice
Thomas C
TC
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D019905:Benzyl Alcohol / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D003198:Computer Simulation; D006736:Horses; D008099:Liver / Q000201:enzymology*; D008958:Models, Molecular; D009243:NAD / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D013816:Thermodynamics
D009243:NAD; D000426:Alcohol Dehydrogenase; D019905:Benzyl Alcohol