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2.) a. Given the following equation and using the Lineweaver-Burk equation find the Vmax and Km...
how do you make a lineweaver-burk plot where the trend line extends backwards? is there a...
how do you make a lineweaver-burk plot where the trend line
extends backwards? is there a way of figuring out how far back it
should extend based of your data ? As well, how do you plot two
sets of data on one graph ? Thank you! (idk if you need to see my
data-> attached below)
Biochemistry Enzyme Kinetics Assignment Four answers for this assignment will be completed in elearn: En in elearn: Enzyme Kinetics Quiz ots but must...
(I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk...
(I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk plot. thanks!) 1. Michaelis-Menten kinetics- use the M-M equation to answer the following: a. An enzyme (5 µM) has a Vmax of 450 mM/min. What is kcat? b. When the substrate concentration is 50 mM, the initial velocity (V0) was measured to be 375 mM/min. Under the conditions described above, calculate the KM. c. Draw the expected Michaelis-Menten plot (label your axes and include...
12. From the Lineweaver-Burk graph given: a. What are the Km and Vmax for the uninhibited...
12. From the Lineweaver-Burk graph given: a. What are the Km and Vmax for the uninhibited case? b. What type of inhibition is occurring? c. Shown on the page after the Lineweaver-Burk plot are semi-qualitative sketches for three V vs. (S) plots. Which one of these most likely corresponds to this particular experiment (A,B or C)? Scani explain th Cant catimer IIIIIIIII IIIIIIIII - -- | - | IIIII We were unable to transcribe this image
You perform a series of enzyme activity assays and then graph the data using a Lineweaver-Burk...
You perform a series of enzyme activity assays and then graph the data using a Lineweaver-Burk plot. You determine the X-intercept is at -0.02 mM-1 and the Y-intercept is at 5.0 (mM/sec)-1. Calculate the Vmax and Km for this enzyme. A. Vmax = 0.20 mM/sec; Km = 50.0 mM B. Vmax = 0.20 mM/sec; Km = ‒50.0 mM C. Vmax = 5.0 mM/sec; Km = 0.02 mM D. Vmax = 5.0 mM/sec; Km = ‒0.02 mM
Michaelis-Menten plot and Lineweaver-Burk plot calculations: Use provided data to generate both M-M and L-B plots....
Michaelis-Menten plot and Lineweaver-Burk plot calculations: Use provided data to generate both M-M and L-B plots. Use scatter plots with markers on Excel: On the M-M Plot: estimate Vmax, KM On the L-B Plot: determine Vmax, KM, keat, kcat/Km. The total enzyme concentration is 5 uM. Graphs can be 1/2 page. Must be computer generated with all axes labeled. Substrate (mM) V. (mM/s) | 1/[S] (mM1) 1/V. (s/mM) 10 | 0 2.73 5.45 8.17 10.9 40.4 0.124 0.181 0.212 0.228...
D-Lactose is the substrate for B-galactosidase. Given Vo = kcat [Et] [S]/km + [S], calculate [S],...
D-Lactose is the substrate for B-galactosidase. Given Vo = kcat [Et] [S]/km + [S], calculate [S], when Km = 4.0 nM, V. = 10.5 M s', kcat = 500 s, and [Et] = 40 uM Calculate the catalytic efficiency. Below is a double-reciprocal plot for an enzyme reaction in the absence and presence of of inhibitor. Give the equation for the line. Calculate Vmax and Km for the enzyme and enzyme plus inhibitor. Which type of inhibition is apparent. 0.10...
11. In Excel, prepare Lineweaver-Burk plots for the behavior of an enzyme for which the following...
11. In Excel, prepare Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available: V, umol/min umol/min (No Inhibitor) S], mM (Inhibitor Present) 3.66 5.12 6.18 6.98 7.60 4.58 6.40 7.72 8.72 9.50 3.0 5.0 7.0 9.0 11.0 a. What are the KM and Vmax values for the inhibited and uninhibited reaction 5 pts. each reaction) b. Is the inhibitor competitive or noncompetitive? (5 pts.) Micheli-Menten) EQUATIONS: VV
8. A chemist obtains the following Lineweaver-Burk plots for an enzyme catalyzed reaction in the ...
Pysical Chemistry! Please show all work thank you.
8. A chemist obtains the following Lineweaver-Burk plots for an enzyme catalyzed reaction in the absence and presence of two different inhibitors, A and B. The linear fit for no inhibition is 302.61.96 x 105 .0 x 10 2.5 x 10 2.0 x 10 1.5x 10 1.0 x10 The linear fit for inhibitor A is: 757.82.03 x 105 No inhibitor And the linear fit for inhibitor B is 50 к 10°- 1015.35.95...
] a. The equation of Lineweaver-Burk double-reciprocal plot of caffeine dehydrogenase-catalyzed reaction is y = 12x...
] a. The equation of Lineweaver-Burk double-reciprocal plot of caffeine dehydrogenase-catalyzed reaction is y = 12x + 3. Calculate Vmax (mmol/s) and Km (mmol/L). b. [5 points] Estimate V for caffeine concentration of 400 mmol/L. c. [10 points] The enzyme caffeine dehydrogenase (Cdh) is an inducible quinone-dependent oxidoreductase. Describe how the addition of caffeine into the culture medium will be detected and transcriptionally regulated by the two-component system in Pseudomonas sp. CBB1.
LINEWEAVER-BURK plot 1. You perform the hydrolysis reaction as required in the lab experiment, and the...
LINEWEAVER-BURK plot 1. You perform the hydrolysis reaction as required in the lab experiment, and the final reading on your blood glucose meter for one of your samples is 385 mg/dL. You need your data to be in units of mm (millimolar, which is millimoles per liter, abbreviated as mmol/L). Show, in a step-by-step conversion, how you would convert 385 mg/dL to the proper answer in mM. 385 mg dlº= ?mm immoles 2. Assuming that the reaction occurred over a...
how do you make a lineweaver-burk plot where the trend line
extends backwards? is there a way of figuring out how far back it
should extend based of your data ? As well, how do you plot two
sets of data on one graph ? Thank you! (idk if you need to see my
data-> attached below)
Biochemistry Enzyme Kinetics Assignment Four answers for this assignment will be completed in elearn: En in elearn: Enzyme Kinetics Quiz ots but must...
12. From the Lineweaver-Burk graph given: a. What are the Km and Vmax for the uninhibited case? b. What type of inhibition is occurring? c. Shown on the page after the Lineweaver-Burk plot are semi-qualitative sketches for three V vs. (S) plots. Which one of these most likely corresponds to this particular experiment (A,B or C)? Scani explain th Cant catimer IIIIIIIII IIIIIIIII - -- | - | IIIII We were unable to transcribe this image
Michaelis-Menten plot and Lineweaver-Burk plot calculations: Use provided data to generate both M-M and L-B plots. Use scatter plots with markers on Excel: On the M-M Plot: estimate Vmax, KM On the L-B Plot: determine Vmax, KM, keat, kcat/Km. The total enzyme concentration is 5 uM. Graphs can be 1/2 page. Must be computer generated with all axes labeled. Substrate (mM) V. (mM/s) | 1/[S] (mM1) 1/V. (s/mM) 10 | 0 2.73 5.45 8.17 10.9 40.4 0.124 0.181 0.212 0.228...
D-Lactose is the substrate for B-galactosidase. Given Vo = kcat [Et] [S]/km + [S], calculate [S], when Km = 4.0 nM, V. = 10.5 M s', kcat = 500 s, and [Et] = 40 uM Calculate the catalytic efficiency. Below is a double-reciprocal plot for an enzyme reaction in the absence and presence of of inhibitor. Give the equation for the line. Calculate Vmax and Km for the enzyme and enzyme plus inhibitor. Which type of inhibition is apparent. 0.10...
11. In Excel, prepare Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available: V, umol/min umol/min (No Inhibitor) S], mM (Inhibitor Present) 3.66 5.12 6.18 6.98 7.60 4.58 6.40 7.72 8.72 9.50 3.0 5.0 7.0 9.0 11.0 a. What are the KM and Vmax values for the inhibited and uninhibited reaction 5 pts. each reaction) b. Is the inhibitor competitive or noncompetitive? (5 pts.) Micheli-Menten) EQUATIONS: VV
Pysical Chemistry! Please show all work thank you.
8. A chemist obtains the following Lineweaver-Burk plots for an enzyme catalyzed reaction in the absence and presence of two different inhibitors, A and B. The linear fit for no inhibition is 302.61.96 x 105 .0 x 10 2.5 x 10 2.0 x 10 1.5x 10 1.0 x10 The linear fit for inhibitor A is: 757.82.03 x 105 No inhibitor And the linear fit for inhibitor B is 50 к 10°- 1015.35.95...
LINEWEAVER-BURK plot 1. You perform the hydrolysis reaction as required in the lab experiment, and the final reading on your blood glucose meter for one of your samples is 385 mg/dL. You need your data to be in units of mm (millimolar, which is millimoles per liter, abbreviated as mmol/L). Show, in a step-by-step conversion, how you would convert 385 mg/dL to the proper answer in mM. 385 mg dlº= ?mm immoles 2. Assuming that the reaction occurred over a...
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