Exposing Hidden Alternative Backbone Conformations in X-ray Crystallography Using qFit.

ABSTRACT: Proteins must move between different conformations of their native ensemble to perform their functions. Crystal structures obtained from high-resolution X-ray diffraction data reflect this heterogeneity as a spatial and temporal conformational average. Although movement between natively populated alternative conformations can be critical for characterizing molecular mechanisms, it is challenging to identify these conformations within electron density maps. Alternative side chain conformations are generally well separated into distinct rotameric conformations, but alternative backbone conformations can overlap at several atomic positions. Our model building program qFit uses mixed integer quadratic programming (MIQP) to evaluate an extremely large number of combinations of sidechain conform

SUBMITTER: Keedy DA 

PROVIDER: S-EPMC4624436 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature