how would you make this plot in excel? CProblem 11 of 15SubmitdadiUsing the following reaction datapoints, construct a Lineweaver-Burkplot for an enzyme with and without anoncompetitive inhibitor by draggingthe points to their relevantcoordinates on the graph and drawinga line of best fit.11mM-11[S]'s mM-1V'with 10 μg per20541036ст5272.5231.2520Answer:

Step 2: Insert Scatter PlotSelect the data you entered.Go to the Insert tab.Click on Scatter Plot…

Answered: C Problem 11 of 15 Submit da di Using…

Biochemistry

9th Edition

ISBN:9781305961135

Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Chapter6: The Behavior Of Proteins: Enzymes

Section: Chapter Questions

Problem 60RE

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Similar questions

MATHEMATICAL You do an enzyme kinetic experiment and calculate a Vmax of 100 mol of product per minute. If each assay used 0.1 mL of an enzyme solution that had a concentration of 0.2 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol?
The energy released by the hydrolysis of ATP is primarily stored between the alpha and beta phosphates equal to -57 kcal/mol harnessed as heat energy by the cell to perform work providing energy to coupled reactions
MATHEMATICAL The enzyme -methylaspartase catalyzes the deamination of -methylaspartate [V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)]. The rate of the reaction was determined by monitoring the absorbance of the product at 240 nm(A240). From the data in the following table, determine KM for the reaction. How does the method of calculation differ from that in Questions 26 and 27?
Nearly all organisms on Earth carry out some form of glycolysis. How does this fact support or not support the assertion that glycolysis is one of the oldest metabolic pathways?
MATHEMATICAL For an enzyme that displays MichaelisMenten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? (a) [S]=KM (b) [S]=0.5KM (c) [S]=0.1KM (d) [S]=2KM (e) [S]=10KM
MATHEMATICAL If a reaction can be written AB, and the G is 20kJmol1, what would the substrate/product ratio have to be for the reaction to be thermodynamically favorable?
MATHEMATICAL For the Vmax obtained in Question 26, calculate the turnover number (catalytic rate constant) assuming that 131024mol of enzyme were used.
Describe the position of the transition state on a vertical energy scale, from low to high, relative to the position of the reactants and products, for both endergonic and exergonic reactions.
Which of the following analogies best describes the induced-fit model of enzyme-substrate binding? a hug between two people a key fitting into a lock a square peg fitting through the square bole and a round peg fitting through the round hole of a children’s toy the fitting together of two jigsaw puzzle pieces
Do you think that the Ea for ATP hydrolysis is relatively low or high? Explain your reasoning.
MATHEMATICAL The kinetic data in the following table were obtained for the reaction of carbon dioxide and water to produce bicarbonate and hydrogen ion catalyzed by carbonic anhydrase: CO2+H2OHCO3+H+ [H. De Voe and G. B. Kistiakowsky, J. Am. Chem. Soc. 83, 274 (1961)]. From these data, determine KM and Vmax for the reaction. CarbonDioxideconcentration(mmolL1)1/Velocity(M1sec)1.252.55.020.00.25036103201031210361030.256
MATHEMATICAL Catalase breaks down hydrogen peroxide about 107 times faster than the uncatalyzed reaction. If the latter required one year, how much time would be needed by the catalase- catalyzed reaction?

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