And as a result of that localized conformational change that basically creates the proper confirmation of the active side and also creates that oxynine hole that is needed to stabilize the tetrahedral intermediate that is formed in that proteolytic reaction that climate Trypsin actually carries out. So we see that proteolytic activation of Chimotrypsinogen causes a local conformational change that allows the active side and the oxygenine hole to actually form. So we conclude that by proteolytically cleaving this inactive Chimotrypcinogen so the entire structure of this Chimetrypsin doesn't actually change too much. But because of a small localized change in this section of that enzyme that creates a perfect active that can fit the substrate molecule and also creates the oxygen hole that will be used by the Chimetrypsin to basically stabilize and decrease that transition state that is formed in that proteolytic reaction that is carried out that is carried out by the digestive enzyme climate trypsin. Now, this is only one of the many different types of digestive enzymes that exist inside our body. And the reason we have these different digestive enzymes is because each digestive enzyme has a slightly different specificity.