But it's the shape of that active side, the s one pocket that determines the specificity of that protease, the type of peptide bond it actually breaks. And so the difference between Chima, Trips and Trypsin and Elastase is not in the type of catalytic triad used, but it's in the shape of that particular s one pocket. The structure of that s one pocket, as we'll see in just a moment, as a result of a slight variation in the s one pocket of Trypsin and Elastase, we see that these other CM proteases cleave other amino acids. So although Trypsin elastics use the same mechanism, so covalent catalysis and acid based catalysis, which we spoke about in the previous lecture, they differ in their specificity. And that has to do to the fact that there is a slight structural difference in the s one pocket in Trypsin as well as elastics. And let's see what these differences are and what they result in.