Absolute binding free energy calculations: on the accuracy of computational scoring of protein-ligand interactions.

ABSTRACT: Calculating the absolute binding free energies is a challenging task. Reliable estimates of binding free energies should provide a guide for rational drug design. It should also provide us with deeper understanding of the correlation between protein structure and its function. Further applications may include identifying novel molecular scaffolds and optimizing lead compounds in computer-aided drug design. Available options to evaluate the absolute binding free energies range from the rigorous but expensive free energy perturbation to the microscopic linear response approximation (LRA/beta version) and related approaches including the linear interaction energy (LIE) to the more approximated and considerably faster scaled protein dipoles Langevin dipoles (PDLD/S-LRA version) as well as the

SUBMITTER: Singh N 

PROVIDER: S-EPMC2868600 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature