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 accurately describes the tertiary structure level of a protein?

The association of multiple polypeptide subunits to form a functional protein complex.

The linear sequence of amino acids in a polypeptide chain.

The regular arrangement of amino acids into α-helices and β-sheets stabilized by hydrogen bonds.

The overall three-dimensional folding of a single polypeptide chain stabilized by interactions among side chains (R groups).

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Verified step by step guidance

Step 1: Understand the hierarchical levels of protein structure. Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. Each level describes a different aspect of the protein's organization.

Step 2: Recall the definition of tertiary structure. The tertiary structure refers to the overall three-dimensional folding of a single polypeptide chain. This folding is stabilized by interactions among the side chains (R groups) of the amino acids.

Step 3: Differentiate tertiary structure from other levels. The primary structure is the linear sequence of amino acids, the secondary structure involves regular arrangements like α-helices and β-sheets stabilized by hydrogen bonds, and the quaternary structure describes the association of multiple polypeptide subunits.

Step 4: Identify the correct description of tertiary structure from the options provided. The correct answer is the one that mentions the three-dimensional folding of a single polypeptide chain stabilized by interactions among side chains (R groups).

Step 5: Recognize the types of interactions stabilizing tertiary structure. These include hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges, which contribute to the protein's overall shape and function.