Final answer:
Upon treatment with trypsin, the peptide Leu-Val-Ala-Arg-Phe-Val-Ala-Leu-Lys-Gly-Arg-Pro-Asp will yield two tetrapeptides, one dipeptide, and one tripeptide, corresponding to option d) 1 dipeptide, 1 tripeptide and 2 tetrapeptides.
Step-by-step explanation:
Trypsin is a proteolytic enzyme that specifically cleaves peptide bonds at the carboxyl side of the amino acids lysine and arginine. Given the peptide sequence Leu-Val-Ala-Arg-Phe-Val-Ala-Leu-Lys-Gly-Arg-Pro-Asp and the specificity of trypsin, we can anticipate where the cleavages will occur.
Cleavage occurs:
- After Arg to yield Leu-Val-Ala-Arg
- After Lys to yield Phe-Val-Ala-Leu-Lys
- After the second Arg to yield Gly-Arg
- No cleavage after Pro because Pro is not a trypsin cleavage site
Therefore, treatment of this peptide by trypsin will result in the formation of two tetrapeptides (Leu-Val-Ala-Arg and Phe-Val-Ala-Leu), one dipeptide (Gly-Arg), and the remaining tripeptide being Pro-Asp since it does not contain internal lysine or arginine residues for trypsin to act on.
Thus, the correct products resulting from the treatment of the peptide with trypsin are: two tetrapeptides, one dipeptide, and one tripeptide. This corresponds to option d) 1 dipeptide, 1 tripeptide and 2 tetrapeptides.