Trypsin cleaves a protein at the
Trypsin cleaves a protein at the
Select an option to attempt
Correct Answer: Option B
Explanation
Trypsin is a serine protease of the digestive system (secreted as trypsinogen from the pancreas, activated by enteropeptidase in the duodenum). It cleaves peptide bonds on the CARBOXYL (C-terminal) side of the basic amino acid residues arginine (Arg, R) and lysine (Lys, K), EXCEPT when followed by proline. The catalytic triad (Ser195, His57, Asp102) acts as a charge relay to hydrolyse the amide bond. Trypsin is widely used in proteomics for peptide mass fingerprinting in mass spectrometry because it produces predictable, well-ionised peptide fragments.