Energy landscape of all-atom protein-protein interactions revealed by multiscale enhanced sampling.

ABSTRACT: Protein-protein interactions are regulated by a subtle balance of complicated atomic interactions and solvation at the interface. To understand such an elusive phenomenon, it is necessary to thoroughly survey the large configurational space from the stable complex structure to the dissociated states using the all-atom model in explicit solvent and to delineate the energy landscape of protein-protein interactions. In this study, we carried out a multiscale enhanced sampling (MSES) simulation of the formation of a barnase-barstar complex, which is a protein complex characterized by an extraordinary tight and fast binding, to determine the energy landscape of atomistic protein-protein interactions. The MSES adopts a multicopy and multiscale scheme to enable for the enhanced sampling of the al

SUBMITTER: Moritsugu K 

PROVIDER: S-EPMC4207830 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature