Chymotrypsin is a digestive enzyme that belongs to the serine protease family and is particularly known for its role in cleaving peptide bonds on the carboxyl side (C-terminus) of aromatic amino acids, which have aryl side chains. The aromatic amino acids that chymotrypsin typically recognizes include phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp).

The given peptide sequence is: Val-Phe-Leu-Met-Tyr-Pro-Gly-Trp-Cys.

We will break down this sequence by identifying where chymotrypsin cleaves:

1. The first cleavage site by chymotrypsin is after Phe (Phenylalanine). Thus, the sequence is cleaved at the C-terminal of Phe, forming: \([\text{Val-Phe}]\, [\text{Leu-Met-Tyr-Pro-Gly-Trp-Cys}]\).
2. The second cleavage site is after Tyr (Tyrosine) as it is also an aromatic amino acid. The resulting segments post-cleavage are: \([\text{Val-Phe-Leu-Met-Tyr}]\, [\text{Pro-Gly-Trp-Cys}]\). On further breakdown: \([\text{Val-Phe-Leu-Met}]\, [\text{Tyr-Pro-Gly-Trp-Cys}]\).
3. The final cleavage site is after Trp (Tryptophan). The cleavage results are: \([\text{Tyr-Pro-Gly-Trp}]\, [\text{Cys}]\).

From these cleavages, we can observe tripeptides (groups of three amino acids). The relevant tripeptides formed are Leu-Met-Tyr and Pro-Gly-Trp.

Let's verify the options provided and see which ones match our analysis:

• Option 1: Leu-Met-Tyr - This tripeptide is formed from the cleavage.
• Option 2: Phe-Leu-Met - This is not a tripeptide formed after cleavage.
• Option 3: Pro-Gly-Trp - This tripeptide is formed from the cleavage.
• Option 4: Tyr-Pro-Gly - This is not a tripeptide formed directly after cleavage.

Therefore, the correct tripeptides formed are Leu-Met-Tyr and Pro-Gly-Trp.