Thank you. I did actually look through this yesterday evening but it didn't explain anything to me.
I'm an undergrad for Human Nutrition doing an intro to Biochemistry - this may be way above my level of understanding as far as chemistry; however, it's frustrating as there's an explanation out there somewhere.
My knowledge goes as far as knowing chymotrypsin cleaves after residues with aromatic sides chains i.e. tryp, tyr and phenyl and trypsin cleaves at residues after positively charged side chains, i.e. arg and lys.
My results show a reaction between the substrate, that contains arg, and chymotrypsin and also between the substrate, that contains phenyl, and trypsin.
Is it something to do with the N-terminal for either? Is arginine is present when activating chymotrypsin from chymotrypsinogen by trypsin?
Trypsin - proline residue at the end or something to do with the acidic residue?
I'm not looking for the answer to be given to me, just a shove in the right direction:)