Answer:
The protease Trypsin would cleave the peptide molecules in the following ways below.
Step-by-step explanation:
Each member of the serine protease family cleaves/cuts the bond after a specific amino acid of the substrate due to that specific amino acid being recognized by a binding structure of the enzyme that is specifically created to bind that specific amino acid. Therefore the protease would cleave the following peptide molecules in the following ways:
- leu-thr-phe-ala-ser would remain unaffected by the protease trypsin as lysine and arginine amino acids to not form part of the peptide molecule.
- trp-tyr-lys-ala-phe would be cleaved by trypsin and become: trp-tyr-lys + ala-phe.
- lys-arg-lys-arg-va would be cleaved to have a product of 2lys + 2arg +va.