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

In general, which option contains the major cooperative interactions driving spontaneous protein folding?

Hydrophobic interactions in the protein core & formation of hydrogen bonds in secondary structures.

Formation of salt bridges & disulfide bonds between R-groups that stabilize key interactions.

Reduced chain conformational entropy.

Restricting surrounding solvent molecules to have less rotational/conformational possibilities.

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Verified step by step guidance

Understand the concept of protein folding: Protein folding is the process by which a protein structure assumes its functional shape or conformation. This process is driven by various interactions within the protein and with its environment.

Identify the major cooperative interactions: The primary forces driving spontaneous protein folding include hydrophobic interactions, hydrogen bonding, salt bridges, and disulfide bonds.

Hydrophobic interactions: These occur when non-polar amino acid side chains aggregate in the interior of the protein, away from the aqueous environment, stabilizing the protein structure.

Hydrogen bonds: These are formed between the backbone atoms in secondary structures like alpha-helices and beta-sheets, contributing to the stability of these structures.

Consider other factors: Reduced chain conformational entropy and solvent molecule restrictions also play roles, but the major driving forces are hydrophobic interactions and hydrogen bonding.