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 …

It is widely accepted that drug–target association and dissociation rates directly affect drug
efficacy and safety. To rationally optimize drug binding kinetics, one must know the atomic …

Large parallel gains in the development of both computational resources and sampling
methods have now made it possible to simulate dissociation events in ligand–protein …

The recent paradigm shift toward the use of the kinetics parameters in place of
thermodynamic constants is leading the computational chemistry community to develop …

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 …

Ligand residence times and binding rates have been found to be useful quantities to
consider during drug design. The underlying structural and dynamic determinants of these …

Understanding ligand dissociation mechanisms at an atomic resolution is a highly desired
but difficult to achieve objective in experiments as well as in computer simulations. Structural …

Studying the pathways of ligand–receptor binding is essential to understand the mechanism
of target recognition by small molecules. The binding free energy and kinetics of protein …

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 …

The protein-ligand residence time, τ, influences molecular function in biological networks
and has been recognized as an important determinant of drug efficacy. To predict τ …