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

2. Water

Biochemistry

2. Water

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Multiple Choice

How does a decrease in pH typically affect chemical bonds and the structure of proteins?

It strengthens disulfide bonds, stabilizing the protein structure.

It has no significant effect on protein structure or chemical bonds.

It increases hydrophobic interactions, causing proteins to fold more tightly.

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

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Verified step by step guidance

Understand the concept of protein structure: Proteins are composed of amino acids linked by peptide bonds, and their structure is stabilized by various interactions, including ionic bonds, hydrogen bonds, hydrophobic interactions, and disulfide bonds.

Recognize the role of pH in protein structure: pH affects the ionization state of amino acid side chains, particularly those with acidic or basic groups, which can alter their ability to form ionic bonds and hydrogen bonds.

Analyze the impact of decreased pH: A lower pH increases the concentration of hydrogen ions (H⁺), which can protonate negatively charged groups (e.g., carboxylate groups) and disrupt ionic bonds between oppositely charged side chains.

Consider the effect on hydrogen bonds: Excess hydrogen ions can interfere with hydrogen bonding by competing for the electron-rich atoms involved in these interactions, destabilizing the protein's secondary and tertiary structure.

Conclude the result of pH decrease: The disruption of ionic and hydrogen bonds leads to protein denaturation, where the protein loses its native structure and function, rather than strengthening disulfide bonds or increasing hydrophobic interactions.