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

Lineweaver-Burk Plot

Biochemistry

6. Enzymes and Enzyme Kinetics

Lineweaver-Burk Plot

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Multiple Choice

To determine the V_max from a Lineweaver-Burk plot you would:

Multiply the reciprocal of the x-axis intercept by -1.

Multiply the reciprocal of the y-axis intercept by -1.

Take the reciprocal of the x-axis intercept.

Take the reciprocal of the y-axis intercept.

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Verified step by step guidance

Understand that a Lineweaver-Burk plot is a double reciprocal plot used to analyze enzyme kinetics, where the x-axis represents 1/[S] (the reciprocal of substrate concentration) and the y-axis represents 1/V (the reciprocal of reaction velocity).

Recall that the Lineweaver-Burk equation is given by:

\frac{1}{V} = \frac{K}{m_{V \max}} \frac{1}{S} + \frac{1}{V}

, where Km is the Michaelis constant and Vmax is the maximum reaction velocity.

Identify that the y-intercept of the Lineweaver-Burk plot corresponds to

\frac{1}{V}

To find Vmax, take the reciprocal of the y-intercept value from the Lineweaver-Burk plot.

By taking the reciprocal of the y-intercept, you obtain Vmax, which represents the maximum rate of the enzymatic reaction when the enzyme is saturated with substrate.