Table of contents

1. A Review of General Chemistry5h 5m
2. Molecular Representations1h 14m
3. Acids and Bases2h 46m
4. Alkanes and Cycloalkanes4h 17m
5. Chirality3h 39m
6. Thermodynamics and Kinetics1h 22m
7. Substitution Reactions1h 48m
8. Elimination Reactions2h 30m
9. Alkenes and Alkynes2h 9m
10. Addition Reactions3h 19m
11. Radical Reactions1h 58m
12. Alcohols, Ethers, Epoxides and Thiols2h 42m
13. Alcohols and Carbonyl Compounds2h 17m
14. Synthetic Techniques1h 26m
15. Analytical Techniques:IR, NMR, Mass Spect7h 3m
16. Conjugated Systems6h 13m
17. Ultraviolet Spectroscopy51m
18. Aromaticity2h 34m
19. Reactions of Aromatics: EAS and Beyond5h 1m
20. Phenols55m
21. Aldehydes and Ketones: Nucleophilic Addition4h 56m
22. Carboxylic Acid Derivatives: NAS2h 51m
23. The Chemistry of Thioesters, Phophate Ester and Phosphate Anhydrides1h 10m
24. Enolate Chemistry: Reactions at the Alpha-Carbon1h 53m
25. Condensation Chemistry2h 9m
26. Amines1h 43m
27. Heterocycles2h 0m
28. Carbohydrates5h 53m
29. Amino Acids4h 20m
30. Peptides and Proteins2h 42m
31. Catalysis in Organic Reactions1h 30m
32. Lipids 2h 50m
33. The Organic Chemistry of Metabolic Pathways2h 52m
34. Nucleic Acids1h 32m
35. Transition Metals6h 14m
36. Synthetic Polymers1h 49m

30. Peptides and Proteins

Peptide Sequencing: Partial Hydrolysis

Organic Chemistry

30. Peptides and Proteins

Peptide Sequencing: Partial Hydrolysis

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Multiple Choice

How many peptide chains does the following peptide produce after being treated with chymotrypsin?
Thr-Lys-Cys-Tyr-His-Asp-Trp-Ile-Val-Phe

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Verified step by step guidance

Understand the role of chymotrypsin: Chymotrypsin is a proteolytic enzyme that specifically cleaves peptide bonds at the carboxyl side of aromatic amino acids such as phenylalanine (Phe), tryptophan (Trp), and tyrosine (Tyr).

Identify the aromatic amino acids in the peptide sequence: Examine the given peptide sequence Thr-Lys-Cys-Tyr-His-Asp-Trp-Ile-Val-Phe and locate the aromatic amino acids. In this sequence, the aromatic amino acids are Tyr, Trp, and Phe.

Determine the cleavage sites: Based on the presence of aromatic amino acids, chymotrypsin will cleave the peptide at the carboxyl side of Tyr, Trp, and Phe. This means the peptide will be cleaved after these amino acids.

Count the resulting peptide fragments: After identifying the cleavage sites, count the number of fragments produced. Each cleavage site results in a new peptide fragment. Since there are three cleavage sites (after Tyr, Trp, and Phe), the peptide will be divided into four fragments.

Conclude the number of peptide chains: The number of peptide chains produced corresponds to the number of fragments after cleavage. Therefore, the peptide will produce four peptide chains after treatment with chymotrypsin.