Now, what's so different between the active Alpha Chimetrypsin and the inactive Chimetrypsinogen? Well, as it turns out, the active side and the oxyanine hole are not formed correctly in this Zymogen form. And what that proteolytic cleavage does is it allows for a localized conformational change to basically take place within this region. 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.