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

Tertiary Structure of Protein

Biochemistry

4. Protein Structure

Tertiary Structure of Protein

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Multiple Choice

Which of the following best depicts the tertiary structures of two globular proteins in an aqueous (water) environment?

Hydrophilic side chains are buried in the interior, while hydrophobic side chains are exposed on the surface.

Hydrophobic side chains are buried in the interior, while hydrophilic side chains are exposed on the surface.

Both hydrophobic and hydrophilic side chains are randomly distributed throughout the protein.

Disulfide bonds are only found on the protein surface.

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Verified step by step guidance

Step 1: Understand the concept of tertiary structure in proteins. Tertiary structure refers to the three-dimensional folding of a protein, which is stabilized by various interactions such as hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bonds.

Step 2: Recall the behavior of hydrophobic and hydrophilic side chains in an aqueous environment. Hydrophobic side chains tend to avoid water and are typically buried in the interior of the protein, while hydrophilic side chains interact favorably with water and are exposed on the surface.

Step 3: Evaluate the given options. The first option states that hydrophilic side chains are buried in the interior, which contradicts the known behavior of hydrophilic residues in water. The second option correctly describes the arrangement of hydrophobic and hydrophilic side chains in globular proteins. The third option suggests random distribution, which does not align with the organized folding of proteins. The fourth option incorrectly states that disulfide bonds are only found on the surface, whereas disulfide bonds can occur in both interior and surface regions.

Step 4: Focus on the correct answer. The correct depiction of tertiary structure in globular proteins in an aqueous environment is that hydrophobic side chains are buried in the interior, while hydrophilic side chains are exposed on the surface. This arrangement minimizes the unfavorable interaction of hydrophobic residues with water and maximizes the favorable interaction of hydrophilic residues with the aqueous environment.

Step 5: Summarize the reasoning. The folding of globular proteins in water is driven by the hydrophobic effect, where hydrophobic residues cluster away from water, forming the protein's core, while hydrophilic residues remain on the surface to interact with the surrounding water molecules.