Ten-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase⋅PhCH2O− complex
AUTOR(ES)
Luo, Jia
FONTE
National Academy of Sciences
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=139189Documentos Relacionados
- Nanosecond time-resolved circular polarization of fluorescence: study of NADH bound to horse liver alcohol dehydrogenase.
- Structure of the complex of active site metal-depleted horse liver alcohol dehydrogenase and NADH.
- Structural and functional zinc in horse liver alcohol dehydrogenase.
- A 5-nanosecond molecular dynamics trajectory for B-DNA: analysis of structure, motions, and solvation.
- Triplex hydration: nanosecond molecular dynamics simulation of the solvated triplex formed by mixed sequences
