Reconciling mediating and slaving roles of water in protein conformational dynamics.

ABSTRACT: Proteins accomplish their physiological functions with remarkably organized dynamic transitions among a hierarchical network of conformational substates. Despite the essential contribution of water molecules in shaping functionally important protein dynamics, their exact role is still controversial. Water molecules were reported either as mediators that facilitate or as masters that slave protein dynamics. Since dynamic behaviour of a given protein is ultimately determined by the underlying energy landscape, we systematically analysed protein self energies and protein-water interaction energies obtained from extensive molecular dynamics simulation trajectories of barstar. We found that protein-water interaction energy plays the dominant role when compared with protein self energy, and thes

SUBMITTER: Zhao L 

PROVIDER: S-EPMC3623917 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature