None Using the following reaction data points, construct aLineweaver-Burk plot by dragging the points to theirrelevant coordinates on the graph and drawing a line ofbest fit. Based on the plot, determine the value of katgiven that the enzyme concentration in this experimentis 5.0 μM.11μΜ[S]'V'SUM-1100.00.10075.00.08050.00.06015.00.03010.00.0255.00.0201/Answer:0.15Click to Draw Line of Best Fit0.1 Movable Points(50.0, 0.060)0:05(10.0, 0.025)(15.0) 0.030)-0.050(5.0,0.020)Keat=11.8476(100.0, 0.100)(75.0, 0.080)Line of Best Fit:y 8.4 x 10 +0.0168.501001/[S]

Lineweaver-Burk Plot Basics:The Lineweaver-Burk plot is a graph that helps understand enzyme…

Answered: Using the following reaction data…

Chemical Principles in the Laboratory

11th Edition

ISBN:9781305264434

Author:Emil Slowinski, Wayne C. Wolsey, Robert Rossi

Publisher:Emil Slowinski, Wayne C. Wolsey, Robert Rossi

Chapter21: Rates Of Chemical Reactions, Ii. A Clock Reaction

Section: Chapter Questions

Problem 2ASA

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How can I isolate mJuce in the equation, Please go step by step mJuce * XJuce = (mJuce-mVapor) *XConcentrate
The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics. Product formed (mmol/min) Substrate added (mmol/L) 217 0.8 325 2 433 4 488 6 647 1000 The Km for this enzyme is approximately: 4 mM. 2 mM. 1 mM. 6 mM. 1000 mM.
Using the data provided use a Michaelis-Menten and Lineweaver-Burk plot to determine the K and Vmax values for enzyme. [9], mM 3.0 4.58 5.0 6.40 7.0 7.72 9.0 8.72 11.0 9.50 [S], mM V, no Inhibitor (Arbitary units) 1 x 10-4 0.026 5 x 10-4 0.092 1.5 x 10-³ 0.136 2.5 x 10-³ 0.150 0.165 5 x 10-3
Please give me very detailed solution.
-3.5 -4 -4.5 Ink -5 -5.5 y=16.137 – 6300.8x R²= 0,99748 -6 -6.5 0.0031 0.0032 0.0033 0.0034 0.0035 0.0036 1T (1/K) Use to above graph to determine the activation energy (Ea) and the value of the frequency factor(A). Do not forget the units.
Table 1 Experiment Temperature of solution Exp k 273 Time for Color change(s) 12345 6 1457 278 1077 288 485 293 359 298 208 303 (equation 6)= k, = 2. 3. n In 1- 47 Determine the value of n (Equation (6)) from the concentrations of the solutions. Plot In 11/n versus 1/T and determine the activation energy for the reaction from the slope. Include the graphs in your report. 4. Determine the pre-exponential factor A from the intercept of your graph. 5. Determine the rate constants k₁ and k₂ at 25°C.
After the neutralization reaction of 42% 0.5 mL nitric acid and 0.28M 18 mL sodium hydroxide, a temperature increase of 15 ° C was observed and the temperature value was determined as 825 cal. According to these results; a) Number of moles of neutralized base ................. ...................... b) Reaction enthalpy .................. ................. Reaction according to enthalpy value ................ .................. c) The constant of the calorimeter in terms of water ............................ ..................... (d (HNO3) = 1.51g / mL; M (HNO3) = 63.01 g / mol) Note: enter only required numerical values and units in the spaces in the question.
Please don't provide handwriting solution
4
8. Data on the speeds of a Michaelis-Menten enzyme reaction v (in micromolar/minute) as a function of the substrate concentration S (in micromolar) has been collected. Your goal is to find a model that fits this data. a) What type of transformation do you need to do for the data so that the transformed data looks like a linear function? b) Assume that the appropriate transformation on the data has been performed and that a linear regression line has been fitted to the transformed data and that its equation is given by Y = 0.501147.X +0.454986 Compute the parameters Vmax and KM and write the model. and KM = v(S) = micromolar minute c) What is the context domain of this function? d) Predict the speed of the reaction (in micromolar/minute) when the concentration is 12.45 micromolar. Round your answer to two decimal places. v(S) = micromolar minute e) What is the maximal speed of the reaction? micromolar minute
For A⟶products, time and concentration data were collected and plotted as shown. [?] (?) t (s) 0.6000.600 00.000.0 0.4840.484 30.030.0 0.4050.405 60.060.0 0.3490.349 90.090.0 order = k = units =
a. Using the graph paper below, to plot the enzyme velocity versus the substrate concentration in the absence of ibuprofen, estimate the Km and Vmax for this enzyme.

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