Hydrogen exchange kinetics changes upon formation of the soybean trypsin inhibitor-trypsin complex.
The hydrogen exchange kinetics of the complex of trypsin-soybean trypsin inhibitor (Kunitz) have been compared to the calculated sum of the exchange kinetics for the inhibitor and trypsin measured separately. The exchange rates observed for the complex are substantially less than the sum of the exchange rates in the two individual proteins. These results cannot be accounted for by changes in intermolecular or intramolecular hydrogen bonding. The decrease in exchange rates in the complex are ascribed to changes in solvent accessibility in the component proteins.
D001550:Benzamidines; D001665:Binding Sites; D006859:Hydrogen; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D046911:Macromolecular Substances; D011485:Protein Binding; D011487:Protein Conformation; D014357:Trypsin / Q000378:metabolism; D014360:Trypsin Inhibitor, Kunitz Soybean; D014361:Trypsin Inhibitors
D001550:Benzamidines; D046911:Macromolecular Substances; D014361:Trypsin Inhibitors; D006859:Hydrogen; D014360:Trypsin Inhibitor, Kunitz Soybean; D014357:Trypsin