Nature Communications (Sep 2018)
Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
Abstract
Trypsin is a serine protease. Here the authors present the high resolution X-ray and neutron diffraction structures of uncomplexed and inhibitor bound trypsin that provide insights into the geometry of H-bonds in the active site of the enzyme and molecular dynamics simulations reveal the kinetics of ligand binding induced desolvation.