Effects of serpin binding on the target proteinase: global stabilization, localized increased structural flexibility, and conserved hydrogen binding at the active site

The effects of serpin binding on the target proteinase particularly on the stabilization, localized enhanced conformational flexibility, and retained hydrogen bonding at the active site were established. Lower stability of rat trypsin toward thermal denaturation in the free enzyme indicated the presence of extensive protein-protein interactions that stabilize the folding process for the complex.