Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

5. Protein Techniques

Chemical Cleavage of Bonds

Biochemistry

5. Protein Techniques

Chemical Cleavage of Bonds

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Multiple Choice

Given the amino acid sequence DAHGHFLKAGMT, what reagent would cleave the last residue, T, from the peptide? That is, one of the products after treatment will be the free amino acid: T.

Trypsin.

Phenyl isothiocyanate.

Cyanogen bromide.

Iodoacetate.

Chymotrypsin.

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Verified step by step guidance

Identify the type of bond that needs to be cleaved to remove the last residue, T, from the peptide sequence DAHGHFLKAGMT. This involves breaking the peptide bond between the last two amino acids, M and T.

Understand the specificity of each reagent listed. Cyanogen bromide is known to cleave at the carboxyl side of methionine residues.

Examine the peptide sequence DAHGHFLKAGMT and locate the methionine (M) residue. In this sequence, M is the penultimate residue.

Recognize that cyanogen bromide will cleave the peptide bond after the methionine residue, resulting in the release of the terminal amino acid, T, as a free amino acid.

Conclude that cyanogen bromide is the appropriate reagent to cleave the last residue, T, from the peptide sequence DAHGHFLKAGMT, as it specifically targets methionine residues.