So let's take a look at how that actually takes place by looking at the following diagram. So, in part A, we basically have that inactive Zymogen, the Chimotrypcinogen. And notice it consists of 145 individual amino acids. So this is not functional because its active side does not have the correct orientation. And the oxyanion hole that is used to basically stabilize the tetrahedral intermediate is not formed. And so what must happen is to actually activate the enzyme activity of this molecule, trypsin and active form another digestive enzyme basically must cleave at a single peptide bond this inactive chymatrypcinogen.