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

6. Enzymes and Enzyme Kinetics

Enzyme Kinetics

Biochemistry

6. Enzymes and Enzyme Kinetics

Enzyme Kinetics

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Multiple Choice

Which of the following is appropriate for initial rate method experiments to analyze an enzyme-catalyzed reaction?

Measuring the rate after the product concentration has plateaued

Using substrate concentrations much lower than the enzyme concentration

Measuring the reaction rate before significant substrate depletion occurs

Allowing the reaction to proceed to equilibrium before measuring the rate

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Verified step by step guidance

Understand the concept of the initial rate method: The initial rate method involves measuring the reaction rate at the very beginning of the reaction, where the substrate concentration is high and product formation is minimal. This ensures that the reaction rate reflects the enzyme's activity without interference from substrate depletion or product accumulation.

Step 1: Eliminate incorrect options. For example, measuring the rate after the product concentration has plateaued is incorrect because the reaction has already reached equilibrium, and the rate is no longer reflective of the enzyme's catalytic activity.

Step 2: Consider the role of substrate concentration. Using substrate concentrations much lower than the enzyme concentration is inappropriate because it can lead to substrate depletion too quickly, making it difficult to measure the initial rate accurately.

Step 3: Focus on the correct condition. Measuring the reaction rate before significant substrate depletion occurs is appropriate because it ensures that the enzyme operates under conditions where the substrate concentration is relatively constant, allowing for accurate determination of the initial rate.

Step 4: Avoid equilibrium conditions. Allowing the reaction to proceed to equilibrium before measuring the rate is incorrect because the reaction rate at equilibrium is zero, and it does not provide information about the enzyme's catalytic efficiency.