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

4. Protein Structure

Peptide Bond

Biochemistry

4. Protein Structure

Peptide Bond

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Multiple Choice

Which of the following peptides is most likely to form a covalently bonded dimer?

Cys-Gly-Ser

Ala-Gly-Leu

Gly-Pro-Tyr

Asp-Val-Lys

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Verified step by step guidance

Step 1: Understand the concept of covalent bonding in peptide dimers. Covalent bonds in peptide dimers are typically formed through disulfide bonds, which occur between the thiol (-SH) groups of cysteine residues.

Step 2: Analyze the peptide sequences provided in the problem. Look for the presence of cysteine (Cys) in the sequences, as it is the amino acid capable of forming disulfide bonds.

Step 3: Identify the peptide sequence that contains cysteine. Among the options provided, only 'Cys-Gly-Ser' contains a cysteine residue, which has the thiol group necessary for forming disulfide bonds.

Step 4: Explain why the other peptide sequences cannot form covalently bonded dimers. 'Ala-Gly-Leu,' 'Gly-Pro-Tyr,' and 'Asp-Val-Lys' do not contain cysteine, so they lack the thiol group required for disulfide bond formation.

Step 5: Conclude that the peptide most likely to form a covalently bonded dimer is 'Cys-Gly-Ser,' due to the presence of cysteine and its ability to form disulfide bonds.