Bayesian refinement of protein structures and ensembles against SAXS data using molecular dynamics.

ABSTRACT: Small-angle X-ray scattering is an increasingly popular technique used to detect protein structures and ensembles in solution. However, the refinement of structures and ensembles against SAXS data is often ambiguous due to the low information content of SAXS data, unknown systematic errors, and unknown scattering contributions from the solvent. We offer a solution to such problems by combining Bayesian inference with all-atom molecular dynamics simulations and explicit-solvent SAXS calculations. The Bayesian formulation correctly weights the SAXS data versus prior physical knowledge, it quantifies the precision or ambiguity of fitted structures and ensembles, and it accounts for unknown systematic errors due to poor buffer matching. The method further provides a probabilistic criterion for

SUBMITTER: Shevchuk R 

PROVIDER: S-EPMC5662244 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature