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.
Goto
K
K
Department of Pathology, Tohoku University School of Medicine, Sendai, Japan.
D000818:Animals; D001665:Binding Sites; D008958:Models, Molecular; D011487:Protein Conformation; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000378:metabolism; D015843:Serpins / Q000737:chemistry; D013381:Subtilisins / Q000737:chemistry; D013499:Surface Properties; D013552:Swine
D015842:Serine Proteinase Inhibitors; D015843:Serpins; D012697:Serine Endopeptidases; D013381:Subtilisins