Addressing the Role of Conformational Diversity in Protein Structure Prediction.

ABSTRACT: Computational modeling of tertiary structures has become of standard use to study proteins that lack experimental characterization. Unfortunately, 3D structure prediction methods and model quality assessment programs often overlook that an ensemble of conformers in equilibrium populates the native state of proteins. In this work we collected sets of publicly available protein models and the corresponding target structures experimentally solved and studied how they describe the conformational diversity of the protein. For each protein, we assessed the quality of the models against known conformers by several standard measures and identified those models ranked best. We found that model rankings are defined by both the selected target conformer and the similarity measure used. 70% of the pro

SUBMITTER: Palopoli N 

PROVIDER: S-EPMC4861349 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature