Describe the strengths/weaknesses of a michaelis menten and line weaver burk plots
Describe the strengths/weaknesses of a michaelis menten and line weaver burk plots
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.
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 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
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...
(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...
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...
The following data were obtained in an enzyme study: Use these data to construct a Michaelis-Menten plot, a Lineweaver-Burk plot, and an Eadie-Hofstee plot. Fit the data in the L-B and E-H plots and use the fit parameters to determine K_M and v_s in each case. Comment on how well the K_Ms and v_ss agree with each other.
How can the Michaelis-Menten constant, be derived from this Lineweaver-Burk plot? Vmax O km = (-1)/(x-intercept) O km = (-1) * (x-intercept) O km = 1/(x-intercept) 0 Km = s;lope
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. S Where v is the velocity or rate, Vmax is the maximum velocity, Km is the +IST Michaelis- Menten constant, and I5 s the substrate concentration. K + S v (uM/min) a) A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (Vo) at different substrate concentrations ([S]) 300 Vmax 250 1/2 Vmax First, move the line labeled "Vmax to a...
The Eadie-Hofstee plot shown below, is an alternative graphical representation of Michaelis-Menten kinetics. t plots the rate (v) versus the ratio of the rate over the substrate concentration (vIS]). This plot is typically used to determine the maximum rate, Vmax, and the Michaelis constant, Km, which can be gleaned from the intercepts and slope. Identify each intercept and the slope in terms of the constants Vmax and Km Eadie-Hofstee Plot y-intercept Slope x-intercept AS