Designing tight-binding ligands is a primary objective of small-molecule drug discovery.
Over the past few decades, free-energy calculations have benefited from improved force …

Accurate in silico prediction of protein–ligand binding affinities has been a primary objective
of structure-based drug design for decades due to the putative value it would bring to the …

Conspectus A principal goal of drug discovery project is to design molecules that can tightly
and selectively bind to the target protein receptor. Accurate prediction of protein–ligand …

Binding free energy calculations based on molecular simulations provide predicted affinities
for biomolecular complexes. These calculations begin with a detailed description of a …

Free energy calculations are rapidly becoming indispensable in structure-enabled drug
discovery programs. As new methods, force fields, and implementations are developed …

Many limitations of current computer-aided drug design arise from the difficulty of reliably
predicting the binding affinity of a small molecule to a biological target. There is thus a strong …

Absolute binding free energy calculations with explicit solvent molecular simulations can
provide estimates of protein-ligand affinities, and thus reduce the time and costs needed to …

Rigorous physics-based methods to calculate binding free energies of protein–ligand
complexes have become a valued component of structure-based drug design. Relative and …

Abstract Structure‐based drug design could benefit greatly from computational
methodologies that accurately predict the binding affinity of small compounds to target …

Nowadays, drug design projects benefit from highly accurate protein–ligand binding free
energy predictions based on molecular dynamics simulations. While such calculations have …