So once again, we see that Trypsin cleaves the peptide between the peptide bond between the arginine 15 and the isolucine 16 producing this active pie Chimetrypsin. Now, this active Pychiamatripsin goes on, reacts with another pikmatripsin and that removes two dipeptides to produce a total of three individual chains. And these three chains, which are held together by disulfide bonds basically constitute that fully functional, fully active Chimotrypsin molecule we call Alpha Chimetrypsin. 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.