The given sequence of the polypeptide Ala-Arg-Tyr-Leu-Arg-Pro-Val-Trp-...
Trypsin cuts at the C terminal of Lys or Arg but next a.a. should not be proline. And, also it is an endonuclease not exonuclease. So 2 fragments will be generated.
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The given sequence of the polypeptide Ala-Arg-Tyr-Leu-Arg-Pro-Val-Trp-...
Answer:
The given polypeptide sequence is Ala-Arg-Tyr-Leu-Arg-Pro-Val-Trp-Lys-Pro.
Introduction:
Trypsin is a protease enzyme that cleaves peptide bonds specifically at the carboxyl side of arginine and lysine residues. When a polypeptide is treated with trypsin, it undergoes proteolysis, resulting in the generation of smaller peptide fragments.
Explanation:
When the given polypeptide sequence is treated with trypsin, it will be cleaved at the carboxyl side of arginine (Arg) and lysine (Lys) residues. Let's analyze the given sequence step by step:
1. Ala-Arg-Tyr-Leu-Arg-Pro-Val-Trp-Lys-Pro
- The first cleavage site for trypsin is after the arginine (Arg) residue at position 2 (Ala-Arg), resulting in two fragments:
- Fragment 1: Ala-Arg
- Fragment 2: Tyr-Leu-Arg-Pro-Val-Trp-Lys-Pro
2. Tyr-Leu-Arg-Pro-Val-Trp-Lys-Pro
- The next cleavage site for trypsin is after the lysine (Lys) residue at position 7 (Tyr-Leu-Arg-Pro-Val-Trp-Lys-Pro), resulting in two fragments:
- Fragment 1: Tyr-Leu-Arg-Pro-Val-Trp-Lys
- Fragment 2: Pro
Therefore, after treatment with trypsin, the given polypeptide sequence will generate a total of 2 fragments.
Summary:
When the polypeptide sequence Ala-Arg-Tyr-Leu-Arg-Pro-Val-Trp-Lys-Pro is treated with trypsin, it will be cleaved at the carboxyl side of arginine and lysine residues. This will result in the generation of two peptide fragments: Ala-Arg and Tyr-Leu-Arg-Pro-Val-Trp-Lys-Pro.