Experimentally resolved structures offer immense insights for drug design but can only provide a static snapshot of the full conformational space that represents the flexible nature of biological systems. Molecular dynamics (MD) simulations approximate such flexibility in silico with a trajectory of atom positions over a series of time steps (frames). These trajectories thereby reveal a more detailed -albeit still incomplete -picture of drug-target recognition and binding by providing access to protein-ligand interaction patterns over time . These insights can for example help in lead discovery to examine the stability and validity of a predicted ligand docking pose, and in lead optimization phases to estimate the effect of a chemical modification on binding affinity.