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

Protein Folding

Biochemistry

4. Protein Structure

Protein Folding

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Multiple Choice

Hydrophobic effects play a major role in the formation of which level of protein structure?

Tertiary structure

Secondary structure

Quaternary structure

Primary structure

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Verified step by step guidance

Understand the concept of hydrophobic effects: Hydrophobic effects refer to the tendency of nonpolar molecules or regions of molecules to avoid water and aggregate together. This is driven by the thermodynamic principle of minimizing the disruption of hydrogen bonding in water.

Review the levels of protein structure: Proteins have four levels of structure—primary, secondary, tertiary, and quaternary. Each level represents a different aspect of protein organization.

Analyze the role of hydrophobic effects in tertiary structure: Tertiary structure involves the three-dimensional folding of a single polypeptide chain. Hydrophobic effects play a major role here as nonpolar side chains of amino acids tend to cluster together in the interior of the protein, away from the aqueous environment, stabilizing the folded structure.

Compare hydrophobic effects in other levels of protein structure: Hydrophobic effects are not significant in primary structure (linear sequence of amino acids) or secondary structure (local folding patterns like α-helices and β-sheets). In quaternary structure, hydrophobic interactions may contribute to the assembly of multiple polypeptide chains, but they are most prominent in tertiary structure.

Conclude that hydrophobic effects are primarily responsible for the formation and stabilization of the tertiary structure of proteins, as this level of structure is where the folding driven by hydrophobic interactions occurs.