PHOENIX: a scoring function for affinity prediction derived using high-resolution crystal structures and calorimetry measurements.

ABSTRACT: Binding affinity prediction is one of the most critical components to computer-aided structure-based drug design. Despite advances in first-principle methods for predicting binding affinity, empirical scoring functions that are fast and only relatively accurate are still widely used in structure-based drug design. With the increasing availability of X-ray crystallographic structures in the Protein Data Bank and continuing application of biophysical methods such as isothermal titration calorimetry to measure thermodynamic parameters contributing to binding free energy, sufficient experimental data exists that scoring functions can now be derived by separating enthalpic (ΔH) and entropic (TΔS) contributions to binding free energy (ΔG). PHOENIX, a scoring function to predict binding affinitie

SUBMITTER: Tang YT 

PROVIDER: S-EPMC3046228 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature