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Multiple Choice
How many peptide chains does the following peptide produce after being treated with chymotrypsin? Thr-Lys-Cys-Tyr-His-Asp-Trp-Ile-Val-Phe
A
1
B
2
C
3
D
4
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Verified step by step guidance
1
Understand the role of chymotrypsin: Chymotrypsin is a proteolytic enzyme that specifically cleaves peptide bonds at the carboxyl side of aromatic amino acids such as phenylalanine (Phe), tryptophan (Trp), and tyrosine (Tyr).
Identify the aromatic amino acids in the peptide sequence: Examine the given peptide sequence Thr-Lys-Cys-Tyr-His-Asp-Trp-Ile-Val-Phe and locate the aromatic amino acids. In this sequence, the aromatic amino acids are Tyr, Trp, and Phe.
Determine the cleavage sites: Based on the presence of aromatic amino acids, chymotrypsin will cleave the peptide at the carboxyl side of Tyr, Trp, and Phe. This means the peptide will be cleaved after these amino acids.
Count the resulting peptide fragments: After identifying the cleavage sites, count the number of fragments produced. Each cleavage site results in a new peptide fragment. Since there are three cleavage sites (after Tyr, Trp, and Phe), the peptide will be divided into four fragments.
Conclude the number of peptide chains: The number of peptide chains produced corresponds to the number of fragments after cleavage. Therefore, the peptide will produce four peptide chains after treatment with chymotrypsin.