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

How does exposure to extreme pH (either high or low) affect the tertiary structure of a protein?

It causes the primary structure to break down into individual amino acids.

It disrupts ionic and hydrogen bonds, leading to denaturation of the protein.

It strengthens disulfide bonds, making the protein more stable.

It has no significant effect on the protein's tertiary structure.

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Verified step by step guidance

Understand the concept of protein tertiary structure: The tertiary structure of a protein is the three-dimensional arrangement of its polypeptide chain, stabilized by various interactions such as hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bonds.

Recognize the role of pH in protein stability: Extreme pH levels (either very high or very low) can alter the ionization state of amino acid side chains, particularly those involved in ionic and hydrogen bonding.

Explain how ionic bonds are affected: At extreme pH, the charges on amino acid side chains may change, disrupting ionic bonds that contribute to the protein's tertiary structure.

Discuss the impact on hydrogen bonds: Extreme pH can also interfere with hydrogen bonding by altering the protonation state of functional groups, further destabilizing the protein's structure.

Conclude with denaturation: The disruption of ionic and hydrogen bonds due to extreme pH leads to the unfolding or denaturation of the protein, which compromises its tertiary structure and functionality.