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

Alpha Helix Disruption

Biochemistry

4. Protein Structure

Alpha Helix Disruption

Previous problemNext problem

Struggling with Biochemistry?

Join thousands of students who trust us to help them ace their exams!Watch the first video

Multiple Choice

At pH 6.8, which of the following peptides is least likely to form an α-helix?
Peptide # 1: RSEDNFGAPKSILWE Peptide # 2: DQKASVEMAVRNSGK

Peptide # 1.

Peptide # 2.

Both peptides are equally likely to form an α-helix.

Neither peptide is likely to form an α-helix.

Previous problemNext problem

Verified step by step guidance

Identify the amino acids in each peptide that are known to disrupt α-helix formation. Common helix breakers include proline (P) and glycine (G).

Examine Peptide #1: RSEDNFGAPKSILWE. Note the presence of proline (P) and glycine (G), which are known to disrupt α-helix formation.

Examine Peptide #2: DQKASVEMAVRNSGK. Check for the presence of proline (P) and glycine (G). This peptide does not contain proline, and glycine is less frequent.

Consider the overall charge and side chain interactions at pH 6.8. Peptide #1 has a higher likelihood of unfavorable interactions due to the presence of charged residues like R (arginine) and E (glutamic acid) in close proximity.

Conclude that Peptide #1 is less likely to form an α-helix due to the presence of helix-breaking residues and potential for disruptive side chain interactions.