Binding, proteolytic, and crystallographic analyses of mutations at the protease - Inhibitor interface of the subtilisin BPN′/chymotrypsin inhibitor 2 complex

Medicine & Life Sciences

• chymotrypsin inhibitor 2 100%
• Subtilisins 77%
• Subtilisin 70%
• Protease Inhibitors 50%
• Mutation 27%
• Acylation 13%
• Catalysis 11%
• Enzymes 10%
• Hydrolysis 9%
• Water 6%

Chemical Compounds

• Chymotrypsin Inhibitor 72%
• Protease Inhibitor 57%
• Mutation 41%
• Crystal Structure 24%
• Acylation 23%
• Transition State 19%
• Catalysis 15%
• Hydrolysis 15%
• Molecule 8%