Aprotinin is a small disulfide-stabilized protein that inhibits selected serine proteases, including trypsin-like enzymes. It illustrates a protein inhibitor that blocks access or productive interaction at a protease active site rather than being a general inhibitor of all proteolysis. Its compact, crosslinked structure also makes it a useful model for studying folding and molecular stability. [ref]
PeptideCutter - Cleavage specificities of selected enzymes and chemicals (ExPASy). protease specificities and inhibitor context
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