Write the equations that describe the Michaelis-Menten and the Lineweaver-Burk double-reciprocal plots. Draw examples of each...
Write the equations that describe the Michaelis-Menten and the Lineweaver-Burk double-reciprocal plots. Draw examples of each plot, demonstrating how Km and Vmax can be determined. On the same graphs, draw another plot where the same enzyme-catalyzed reaction is subjected to inhibition by a competitive inhibitor.
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Write the equations that describe the Michaelis-Menten and the
Lineweaver-Burk double-reciprocal plots. Draw examples of each...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is give...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
2. If an inhibitor competitively inhibits an enzyme, use Michaelis-Menten and Lineweaver-Burk plots to illustrate how...
2. If an inhibitor competitively inhibits an enzyme, use Michaelis-Menten and Lineweaver-Burk plots to illustrate how the enzyme kinetics differ in the presence and absence of the inhibitor. (20 pts)
(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...
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...
The Lineweaver-Burk plots shown below are for enzyme catalyzed reactions. The reaction without and inhibitor is...
The Lineweaver-Burk plots shown below are for enzyme catalyzed reactions. The reaction without and inhibitor is shown in blue. The reaction with an inhibitor is shown in red. Identify the type of inhibition in each plot. with I with I 1/vo without I without I 1/[S] 1/[S] with without I without I 1/[S] 1/[S] with I without I 1/[S] Problem 4 For each plot above describe how Km and Vmax are affected by the inhibitor.
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 to determine Vinas, KM, kcat, kcat/KM. The total enzyme concentration is 5 μM. Graphs can be 2 page. Must be computer generated with all axes labeled. Substrate (mM Vo (mM/s) 2.73 5.45 8.17 10.9 40.4 0.124 0.181 0.212 0.228 0.303
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equatio...
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equation as shown below: V0 = (-Km) V0 / [S] + Vmax a). Please derive the Eadie-Hofstee equation starting from the Michaelis-Menten equation. b). The Vmax and Km of the enzyme catalyzed reaction can be derived from a plot of V0 versus V0/[S]. Please draw one of these plots and explain how do you use it to derive Vmax and Km. c). Please draw a...
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
o Flipped class: Michaelis-Menten vs. Lineweaver-Burk 10 Essentially, we'll duplicate the error estimates from (A) a...
o Flipped class: Michaelis-Menten vs. Lineweaver-Burk 10 Essentially, we'll duplicate the error estimates from (A) a nonlinear fit and (B) a nonlinear function transformed into linear form in Matlab. 1) Use Matlab to generate synthetic data obeying the Michaelis-Menten equation i.e. find dP/dt for [S] = 1:20. Add noise to the data (rand or randn or normmd). Use Vmax-1, km-5 2) Plot the data points (dP/dt vs [S]) that you've obtained. Fit the data (model1:- fitnlm(x,y.modelname,jnitialguesses). Output the estimated Vmax...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
2. If an inhibitor competitively inhibits an enzyme, use Michaelis-Menten and Lineweaver-Burk plots to illustrate how the enzyme kinetics differ in the presence and absence of the inhibitor. (20 pts)
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...
The Lineweaver-Burk plots shown below are for enzyme catalyzed reactions. The reaction without and inhibitor is shown in blue. The reaction with an inhibitor is shown in red. Identify the type of inhibition in each plot. with I with I 1/vo without I without I 1/[S] 1/[S] with without I without I 1/[S] 1/[S] with I without I 1/[S] Problem 4 For each plot above describe how Km and Vmax are affected by the inhibitor.
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 to determine Vinas, KM, kcat, kcat/KM. The total enzyme concentration is 5 μM. Graphs can be 2 page. Must be computer generated with all axes labeled. Substrate (mM Vo (mM/s) 2.73 5.45 8.17 10.9 40.4 0.124 0.181 0.212 0.228 0.303
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
o Flipped class: Michaelis-Menten vs. Lineweaver-Burk 10 Essentially, we'll duplicate the error estimates from (A) a nonlinear fit and (B) a nonlinear function transformed into linear form in Matlab. 1) Use Matlab to generate synthetic data obeying the Michaelis-Menten equation i.e. find dP/dt for [S] = 1:20. Add noise to the data (rand or randn or normmd). Use Vmax-1, km-5 2) Plot the data points (dP/dt vs [S]) that you've obtained. Fit the data (model1:- fitnlm(x,y.modelname,jnitialguesses). Output the estimated Vmax...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
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