Ensemble-based characterization of unbound and bound states on protein energy landscape.

ABSTRACT: Physicochemical description of numerous cell processes is fundamentally based on the energy landscapes of protein molecules involved. Although the whole energy landscape is difficult to reconstruct, increased attention to particular targets has provided enough structures for mapping functionally important subspaces associated with the unbound and bound protein structures. The subspace mapping produces a discrete representation of the landscape, further called energy spectrum. We compiled and characterized ensembles of bound and unbound conformations of six small proteins and explored their spectra in implicit solvent. First, the analysis of the unbound-to-bound changes points to conformational selection as the binding mechanism for four proteins. Second, results show that bound and unbound

SUBMITTER: Ruvinsky AM 

PROVIDER: S-EPMC3690713 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature