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Trypsin digests protein(polypeptide) by cleaving the peptide chain at specific sites. Trypsin cleaves the peptide chain after Lysine(K) or Arginine(R) residues (amino acids) except when followed by a Proline(P) residue. Generally, the tryptic digestion leaves behind the protein as peptide chains having none or one Lysine or Arginine residue.

This property of trypsin is widely used to study the protein primary structure and identification of proteins by analysing the resultant peptides using mass sepectrometry (MS).

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Q: How does trypsin digest protein?
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Related questions

What do Trypsin and chymotrypsin digest?

Trypsin breaks down Peptides to Amino Acids


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It is a digestive enzyme that your pancreas produces, enables you to digest the protein you eat. If your pancreas is not producing enough trypsin, you may experience malabsorption, a digestive problem.Read more [related links]


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