Hydrophobic accessible surface areas are proportional to binding energies of serine protease-protein inhibitor complexes.

For analysis of enzyme-protein inhibitor interactions, we calculated the buried hydrophobic and hydrophilic accessible surface areas (ASAs) of enzymes and primary contact regions. In the five enzyme-protein inhibitor complexes so far analyzed, we found that the hydrophobic ASAs buried between the enzyme and the primary contact region are proportional to their experimental binding energies. This finding indicates that the hydrophobic interaction drives the binding of enzymes with protein inhibitors.