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
Describe the assumptions that went into the derivation of the Michaelis-Menten equation.
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...