Highlights•Drug-target binding kinetics contribute to drug efficacy.•Many molecular dynamics
approaches to studying binding kinetics have been reported.•High quality datasets enable …

Protein–ligand binding affinity reflects the equilibrium thermodynamics of the protein–ligand
binding process. Binding/unbinding kinetics is the other side of the coin. Computational …

The determination of drug residence times, which define the time an inhibitor is in complex
with its target, is a fundamental part of the drug discovery process. Synthesis and …

The prediction of drug–target binding and unbinding kinetics that occur on time scales
between milliseconds and several hours is a prime challenge for biased molecular …

Kinetic and thermodynamic ligand–protein binding parameters are gaining growing
importance as key information to consider in drug discovery. The determination of the …

The dissociation of ligands from proteins and other biomacromolecules occurs over a wide
range of timescales. For most pharmaceutically relevant inhibitors, these timescales are far …

The prediction of protein-protein kinetic rate constants provides a fundamental test of our
understanding of molecular recognition, and will play an important role in the modeling of …

Drug-target residence time has emerged as a key selection factor in drug discovery since
the binding duration of a drug molecule to its protein target can significantly impact its in vivo …

The prediction of ligand efficacy has long been linked to thermodynamic properties such as
the equilibrium dissociation constant, which considers both the association and the …

Accurately predicting protein–ligand binding affinities can substantially facilitate the drug
discovery process, but it remains as a difficult problem. To tackle the challenge, many …