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0.35 0.3 0.25 0.2 0.15 0.1 0.05 0.1 0.2 0.3 0.4

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Is the inhibitor competitive uncompetitive or non competitive? Why?
**Michaelis-Menten Plot Explanation** *Figure 11* displays a Michaelis-Menten plot, a common representation in enzyme kinetics. This plot is created using an Excel worksheet, emphasizing how experimental data can be visualized and analyzed. **Data Table** The table consists of several columns: - **A (Ethanol - M)**: Lists ethanol concentrations in molarity ranging from 0.06 to 0.5. - **B (Vo)**: Shows the initial reaction velocities corresponding to each ethanol concentration, measured in appropriate units like microMoles/min or similar. - **C (Calc Vo)**: Represents the calculated initial velocities based on the Michaelis-Menten equation. - **D**: The delta values (difference between actual and calculated velocities). - **Rows 14-16**: Display constants used in calculations: - Km = 0.04 - Vmax = 0.17 **Graph Explanation** The chart depicted below the data table compares actual initial velocities (Vo) and calculated velocities (Calc Vo): - The **x-axis** represents ethanol concentration (M). - The **y-axis** measures the initial reaction velocity. - **Blue diamonds**: Plot the actual initial velocities obtained from experimental data. - **Red curve**: Represents the calculated velocities using the Michaelis-Menten model, demonstrating how the model fits the experimental data. **Key Observations** - This plot helps visualize how well the model predicts experimental results. - The alignment (or deviation) of blue diamonds from the red curve indicates the accuracy of the Michaelis-Menten equation under given conditions. - Such plots are integral for understanding enzyme behavior in response to substrate concentration changes.
Transcribed Image Text:**Michaelis-Menten Plot Explanation** *Figure 11* displays a Michaelis-Menten plot, a common representation in enzyme kinetics. This plot is created using an Excel worksheet, emphasizing how experimental data can be visualized and analyzed. **Data Table** The table consists of several columns: - **A (Ethanol - M)**: Lists ethanol concentrations in molarity ranging from 0.06 to 0.5. - **B (Vo)**: Shows the initial reaction velocities corresponding to each ethanol concentration, measured in appropriate units like microMoles/min or similar. - **C (Calc Vo)**: Represents the calculated initial velocities based on the Michaelis-Menten equation. - **D**: The delta values (difference between actual and calculated velocities). - **Rows 14-16**: Display constants used in calculations: - Km = 0.04 - Vmax = 0.17 **Graph Explanation** The chart depicted below the data table compares actual initial velocities (Vo) and calculated velocities (Calc Vo): - The **x-axis** represents ethanol concentration (M). - The **y-axis** measures the initial reaction velocity. - **Blue diamonds**: Plot the actual initial velocities obtained from experimental data. - **Red curve**: Represents the calculated velocities using the Michaelis-Menten model, demonstrating how the model fits the experimental data. **Key Observations** - This plot helps visualize how well the model predicts experimental results. - The alignment (or deviation) of blue diamonds from the red curve indicates the accuracy of the Michaelis-Menten equation under given conditions. - Such plots are integral for understanding enzyme behavior in response to substrate concentration changes.
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