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Chapter 19: Problem 11

The octapeptide angiotensin II has the sequence Asp-Arg-Val-Tyr-Ile-His- ProPhe. What fragments would result if angiotensin II were cleaved with trypsin? With chymotrypsin?

Short Answer

Expert verified
Trypsin cleaves into Asp-Arg and Val-Tyr-Ile-His-Pro-Phe. Chymotrypsin cleaves into Asp-Arg-Val-Tyr, Ile-His-Pro, and Phe.

Step by step solution

01

Understanding the Cleaving Role of Trypsin

Trypsin is an enzyme that specifically cleaves peptide bonds at the carboxyl side of lysine (Lys, K) and arginine (Arg, R) residues, except when either is followed by proline (Pro, P). In the sequence Asp-Arg-Val-Tyr-Ile-His-Pro-Phe, trypsin will cleave after Arg.
02

Applying Trypsin Cleavage to Angiotensin II

Angiotensin II sequence is Asp-Arg-Val-Tyr-Ile-His-Pro-Phe. With trypsin, we cleave at the carboxyl side of Arg resulting in the fragments: Asp-Arg and Val-Tyr-Ile-His-Pro-Phe.
03

Understanding the Cleaving Role of Chymotrypsin

Chymotrypsin is an enzyme that cleaves at the carboxyl side of aromatic amino acids phenylalanine (Phe, F), tyrosine (Tyr, Y), and tryptophan (Trp, W). In the given sequence, chymotrypsin will cleave after Tyr and Phe.
04

Applying Chymotrypsin Cleavage to Angiotensin II

For the sequence Asp-Arg-Val-Tyr-Ile-His-Pro-Phe, chymotrypsin will cleave after Tyr and Phe, resulting in the fragments: Asp-Arg-Val-Tyr, Ile-His-Pro, and Phe.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Trypsin Enzyme
Trypsin is a powerful digestive enzyme, primarily produced in the pancreas. Its main role is to help in protein digestion by breaking down proteins into smaller peptides. One unique feature of trypsin is its specificity, meaning it only acts at certain points within a protein chain.
  • Cleaving Specificity: Trypsin targets peptide bonds located after lysine (Lys) and arginine (Arg) amino acids. However, it does not cleave if these residues are followed by a proline (Pro) residue.
  • Application in Peptide Cleavage: This property is useful in scientific laboratories for studying protein structures by generating specific peptide fragments.
In our exercise with the octapeptide angiotensin II, trypsin selectively cleaves after the arginine (Arg) residue, splitting the sequence into two smaller fragments.
Chymotrypsin Enzyme
Chymotrypsin is another crucial enzyme in the digestive system. It differs from trypsin in its specificity, targeting different points within protein chains. It is also produced in the pancreas and plays a significant role in protein digestion.
  • Cleaving Specificity: Chymotrypsin targets aromatic amino acids such as phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp). It cleaves at the carboxyl side of these residues.
  • Role in Protein Analysis: Chymotrypsin鈥檚 ability to hydrolyze proteins at specific points makes it useful for analyzing protein structures and sequences.
In the case of angiotensin II, chymotrypsin cleaves after tyrosine (Tyr) and phenylalanine (Phe), producing three distinct peptide fragments.
Amino Acid Sequence
An amino acid sequence describes the order of amino acids in a protein or peptide, which is critical in determining its function and structure.
  • Importance of Sequence: The sequence dictates the protein's shape and how it interacts with other molecules. Even a slight change can significantly alter its function.
  • Notation and Abbreviation: Each amino acid is often represented by either a three-letter abbreviation or one-letter code. This practice simplifies the process of documenting sequences.
In angiotensin II, knowing each amino acid and their positions allows us to predict the result of enzymatic cleavage with precise reactions.

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Most popular questions from this chapter

Give the amino acid sequence of hexapeptides that produce the following sets of fragments on partial acid hydrolysis: (a) Arg. Gly, lle, Leu, Pro, Val gives Pro-Leu-Gly, Arg-Pro, Gly-Ile-Val (b) \(\mathrm{N}, \mathrm{L}, \mathrm{M}, \mathrm{W}, \mathrm{V}_{2}\) gives \(\mathrm{V}-\mathrm{L}, \mathrm{V}-\mathrm{M}-\mathrm{W}, \mathrm{W}-\mathrm{N}-\mathrm{V}\)

Leuprolide is a synthetic nonapeptide used to treat both endometriosis in women and prostate cancer in men. (a) Both C-terminal and N-terminal amino acids in leuprolide have been structurally modified. Identify the modifications. (b) One of the nine amino acids in leuprolide has o stereochemistry rather than the usual \(\mathrm{L}\). Which one? (c) Write the structure of leuprolide using both one- and three-letter abbreviations. (d) What charge would you expect leuprolide to have at neutral \(\mathrm{pH}\) ?

Show how you could use the acetamidomalonate method to prepare the following amino acids: (a) Leucine (b) Tryptophan

What does the prefix " \(\alpha\) " mean when referring to an \(\alpha\) -amino acid?

Except for cysteine, only \(S\) amino acids occur in proteins. Several \(R\) amino acids are also found in nature, however. \((R)\) -Serine is found in earthworms, and ( \(R\) )-alanine is found in insect larvae. Draw the structures of \((R)\) -serine and \((R)\) -alanine. Are these \(\mathrm{D}\) or \(\mathrm{L}\) amino acids?
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