Protein-protein binding affinity prediction on a diverse set of structures
Abstract
Accurate binding free energy functions for protein-protein interactions are imperative for a wide range of purposes. Their construction is predicated upon ascertaining the factors that influence binding and their relative importance. A recent benchmark of binding affinities has allowed, for the first time, the evaluation and construction of binding free energy models using a diverse set of complexes, and a systematic assessment of our ability to model the energetics of conformational changes.
Full text links
Publisher website (DOI) 10.1093/bioinformatics/btr513
Europe PubMed Central 21903632
Pubmed 21903632
Keywords
Type of publication