Network of Conformational Transitions Revealed by Molecular Dynamics Simulations of the Carbonic Anhydrase II Apo-Enzyme.

ABSTRACT: Human carbonic anhydrase II (HCA II) is an enzyme that catalyzes the reversible hydration of CO₂ into bicarbonate (HCO₃^-) and a proton (H⁺) as well as other reactions at an extremely high rate. This enzyme plays fundamental roles in human physiology/pathology, such as controlling the pH level in cells and so on. However, the binding mechanism between apo-HCA II and CO₂ or other ligands as well as related conformational changes remains poorly understood, and atomic investigation into it could promote our understanding of related internal physiological/pathological mechanisms. In this study, long-time atomic molecular dynamics simulations as well as the clustering and free-energy analysis were performed to reveal the dynamics of apo-HCA

SUBMITTER: Ma H 

PROVIDER: S-EPMC6045336 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature