ANATOMY

Detailed explanation-1: -Trypsin cleaves the peptide bond between the carboxyl group of arginine or the carboxyl group of lysine and the amino group of the adjacent amino acid. The rate of cleavage occurs more slowly when the lysine and arginine residues are adjacent to acidic amino acids in the sequence or cystine.

Detailed explanation-2: -Trypsin has become the gold standard for protein digestion to peptides for shotgun proteomics. Trypsin is a serine protease. It cleaves proteins into peptides with an average size of 700-1500 daltons, which is in the ideal range for MS (Laskay et al., 2013).

Detailed explanation-3: -So, the correct answer is ‘true’.

Detailed explanation-4: -Of these five components, pepsin is the principal enzyme involved in protein digestion. It breaks down proteins into smaller peptides and amino acids that can be easily absorbed in the small intestine.

Detailed explanation-5: -Trypsin breaks down the proteins into smaller peptides by hydrolysis reaction. It secretes as an inactive form of trypsinogen, which further gets active to act.