Trypsin is a digestive enzyme of serine protease group. It is considered an endopeptidase dase, i.e., the cleavage occurs within the polypeptide chain rather than at the termi nal amino acids located at the ends of polypeptides. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine (K) or arginine (R), except when either is followed by proline (P) on the C-terminal side or preceded by aspartic acid (D) on the N-terminal side. It is also known that only surface-accessible Kor R are cleaved by the enzyme. Otherwise cleavable amino acids, K and/or 'R if buried inside, cannot be recognized and cleaved by the enzyme trypsin. A fragment of a protein has the following sequence of amino acids that may lead to two different structures P1 and P2 from the same peptide. In P1, the peptide is linear; while in P2the peptide is folded with 26th amino acid lysine (K) buried inside.
(see the picture attached for the amino acids order)
Following a trypsin digestion, the number of peptide fragments that will be formed for P1 and P2, respectively are??
Answers
Answer:
Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins.[2][3] Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.[4] Trypsin was discovered in 1876 by Wilhelm Kühne and was named from the Ancient Greek word for rubbing since it was first isolated by rubbing the pancreas with glycerin.
Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins.[2][3] Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.[4] Trypsin was discovered in 1876 by Wilhelm Kühne and was named from the Ancient Greek word for rubbing since it was first isolated by rubbing the pancreas with glycerin.[5]