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

Quaternary Structure

Biochemistry

4. Protein Structure

Quaternary Structure

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Multiple Choice

Which type of bond is predominantly involved in stabilizing the quaternary structure of proteins?

Peptide bonds

Glycosidic bonds

Hydrophobic interactions

Phosphodiester bonds

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Verified step by step guidance

Understand the quaternary structure of proteins: The quaternary structure refers to the arrangement and interaction of multiple polypeptide chains (subunits) in a protein complex. It is stabilized by various types of interactions between these subunits.

Review the types of bonds and interactions: Peptide bonds are covalent bonds that link amino acids within a single polypeptide chain, forming the primary structure. Glycosidic bonds are found in carbohydrates, linking sugar molecules. Phosphodiester bonds are present in nucleic acids, connecting nucleotides. Hydrophobic interactions occur when nonpolar side chains cluster together to avoid water, contributing to protein folding and stability.

Focus on hydrophobic interactions: In the quaternary structure, hydrophobic interactions play a key role in stabilizing the protein complex. Nonpolar amino acid side chains from different subunits aggregate to minimize exposure to water, creating a stable core.

Relate hydrophobic interactions to protein stability: These interactions help maintain the structural integrity of the protein complex by reducing the free energy of the system and promoting proper subunit assembly.

Conclude that hydrophobic interactions are the predominant force stabilizing the quaternary structure of proteins, as they facilitate the association of subunits in a water-based environment.