Dynamics of ordered water in interfacial enzyme recognition: bovine pancreatic phospholipase A2.

Slippery when wet: Water molecules at the interface between a protein (e.g. bovine pancreatic phospholipase A2) and a micellar substrate act as a lubricant and facilitate movement and binding of the protein at the surface (see picture). Studies of the hydration dynamics before and after complexation reveal that these interactions are crucial for enzymatic function.