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

1. Introduction to Biochemistry

Proteins

Biochemistry

1. Introduction to Biochemistry

Proteins

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Multiple Choice

In a globular protein, which type of interaction is primarily responsible for stabilizing its tertiary structure?

Peptide bonds

Hydrophobic interactions

Glycosidic linkages

Phosphodiester bonds

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Verified step by step guidance

Understand the concept of tertiary structure in proteins: The tertiary structure refers to the three-dimensional folding of a protein, which is stabilized by various interactions between the side chains of amino acids.

Review the types of interactions that contribute to protein stability: These include hydrophobic interactions, hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges.

Focus on hydrophobic interactions: Hydrophobic interactions occur when nonpolar side chains of amino acids cluster together in the interior of the protein, away from the aqueous environment. This minimizes the exposure of hydrophobic regions to water and contributes significantly to the stability of the tertiary structure.

Eliminate incorrect options: Peptide bonds are responsible for linking amino acids in the primary structure, glycosidic linkages are found in carbohydrates, and phosphodiester bonds are present in nucleic acids. None of these are directly involved in stabilizing the tertiary structure of proteins.

Conclude that hydrophobic interactions are the primary force stabilizing the tertiary structure of globular proteins, as they play a key role in maintaining the protein's folded conformation in an aqueous environment.