16. Use the Michaelis-Menten graph to estimate Va and Ku. Show the units. Use the Lineweaver...
The equation that describes the above Michaelis-Menten curve: Vo TS]+K Vmax [S] Michaelis-Menten Equation Lineweaver and Burke manipulated the Michaelis-Menten equation to yield: Ko V I S Vmax [S] Lineweaver-Burke Equation Linewenver Burke Equation If you plot 1/ V. vs. 1/[S], you get the following Lineweaver-Burke plot: 1/V. Slope = km/Vmax Intercept = -1/KM -Intercept = 1/Vmax 1/[S] Which is easier to calculate values for Km and Vmax, using the linear (y=mx+b) Lineweaver-Burke Plot or the Michaelis-Menten curve?
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...
(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. 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...
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
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...
how we can solve q2
2. a) The Michaelis-Menten mechanism is +KTERE] - @s→Es (rateco nstant kl) ク ES→ E + S (rate constant k2) E S ES-XⓟHE) orate constant k3) So d[PVdt- k3[ES] Use the steady state approximation to show [El/[ES] (k2+k3)/(k1[S] b) let Km=(k2+k3)/kl and show that you get the expression ·J [EVIES]-Km/[S] c) We will talk in class about how this information eventually gives rise the expression d[P]/dt-k3E][S/(Km +IS) Usually [S>>Km. Show what this equation simplifies to...
Please show how to calculate Km and Vmax for no inhibitor/low
inhibitor given graph. Show how to solve for a.,a/a etc.
Lineweaver Burk #4: No inhibitor, Low inhibitor 0.2 ▲ No inhibitor Low inhibitor 0.15 0.05 0.2 0.15 0.1 0.05 0.05 0.1 0.15 02 5 1/IS] in units of 1/mM Fill in the blanks. Show your work. No inhibitor Kmno Vmax,o- Vmax,w = ๙ Vmax,o Solve for ๙ inhibitor Krmkw =픕Km,o Solve for 픕 Hint treat, as a single number....
1. Show, using the Michaelis-Menten equation, that when [S] >>> Km, vo = Vmax. Show, using the M-M equation that when [S] <<<Km, vo =[S][Et]kcat/Km. 2. What is Vmax? Provide both a mathematical and written description of Vmax? How can Vmax be experimentally altered? How can we use Vmax to determine the turnover number (kcat) of an enzyme-catalyzed reaction? What is the major challenge of determining Vmax from an Michaelis-Menten plot?
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as a function of substrate concentration; label both axes. Write the associated Michaelis-Menton equation and show the location of Km and Vmax on your graph. b. Draw a second graph showing the classic Lineweaver-Burk plot; label both axes. Show the location of Km and Vmax on your graph. Discuss which plot is the most useful to determine Vmax. Draw a second line on each graph...