Step 1: Understand the specificity of chymotrypsin.
Chymotrypsin is a protease that cleaves peptide bonds on the carboxyl side of aromatic amino acids, such as phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp).
Step 2: Identify the cleavage sites.
In the given sequence, chymotrypsin will cleave after:
- Phe (position 5)
- Trp (position 2)
- Tyr (position 9)
The sequence contains 3 cleavage sites, resulting in 4 fragments.
Step 3: Conclusion.
The number of peptide fragments generated after treatment with chymotrypsin is 4.
Which one of the following matches is CORRECT between the inhibitors given in Group A with their modes of action in Group B?
\[\begin{array}{|c|c|} \hline Group A & Group B \\ \hline \text{(P) Antimycin A} & \text{(i) Inhibits cytochrome c oxidase} \\ \hline \text{(Q) Amytal} & \text{(ii) Blocks electron transfer from cyt b to cyt c1} \\ \hline \text{(R) Carbon monoxide} & \text{(iii) Inhibits adenine nucleotide translocase} \\ \hline \text{(S) Atractyloside} & \text{(iv) Prevents electron transfer from Fe-S centers of complex 1 to ubiquinone} \\ \hline \end{array}\]