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Below is a Lineweaver-Burk plot of enzyme A. What is the Km of this enzyme? (round...
3. Below is a Lineweaver-Burke plot of an enzyme reaction in the presence and absence of an inhibitor. 2.4 2.3 2.2 2.1 2 1.9 1.8 1.7 1.6 1.5 1.4 1.3 1.2 1.1 1 0.9 0.8 < 0.7 0.6 0.5 0.4 0.3 0.2 0.1 0 -0.1 -0.2 -0.3 -0.4 -0.5 -0.6 -0.7 -0.8 . . . . . -1 -0.9 -0.8 -0.7 -0.6 -0.5 -0.4 -0.3 -0.2 -0.1 O 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1 1.1 1/[S]...
intelligent control systems fuzzy logic based contril 0.8 0.7 04 0.3 0.2 0.3 b) Plot the ou a) Plot the output: -BUB 1.0 0.9 0.9 0.8 0.7 0.6 0.5 0.4 0.3 0.5 0.4A 0.3 0.2 0.2 0.17 0.1 c) Determine the defuzzified output y, by using I. Center of Gravity Method (COG) Height Method (H) II. + 1 (0.5)+3 05)+ 5(0.1) 6() 0.8 0.7 04 0.3 0.2 0.3 b) Plot the ou a) Plot the output: -BUB 1.0 0.9 0.9...
N- 0.9 0.8 0.7 (iii) The Michaelis-Menten plot for the reaction of aminobenzene with an enzyme that has a key Glutamic acid residue in the active site is shown on the right. Estimate Km for the reaction of aminobenzene at both pH values and explain in terms of forces why the plots might be different 0.6 Aminobenzene 0.4 0.3 0.2 A 0.1 TA OR 0 10 20 30 40 50 60 70 80 90 10 [L] UM --pH=4.0 HpH=8.0
5. What is the slope of the best fit line for the plot of a vs. sin. What is the value of a at sine-1? How are these two values related? #1 Incline Angle 0-2° (m/s) 0.22 Time Interval (s) Displaceent (m) Average Velocity Average Acceleration 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0 m/s/s 0.021 0.022 0.023 0.024 0.025 0.027 0.029 0.030 0.032 0.033 0.1 0.24 0.25 0.27 0.29 0.30 0.32 0.33 0.2 0.2 0.1 0.2 Average...
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
For a report, after plotting the lineweaver-burk plot for a protease enzyme with and without inhibitor. It shows that the km value increases in the presence of inhibitor and Vmax decreases. what type of inhibition is it? The inhibitor is an azide.
3. Make a plot of a vs. sin6 fon linear graph and draw a best fit line through the data. Extend the best fit line so that it intersects the point at sin@ = 1 . #1 Incline Angle 0-2° (m/s) 0.22 Time Interval (s) Displaceent (m) Average Velocity Average Acceleration 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0 m/s/s 0.021 0.022 0.023 0.024 0.025 0.027 0.029 0.030 0.032 0.033 0.1 0.24 0.25 0.27 0.29 0.30 0.32 0.33...
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...
Provide answers to the following questions using complete sentences. 1. Make a plot of vavg vs. r on linear graph paper for each set of data. Draw a best fit line through each set of data on the plot. 2. What is the slope of each best fit line for each set of data in the plot of vavg VS. ? What does this slope represent? 3. Make a plot of a vs. sin6 fon linear graph and draw a...
1. Which graph(s) can be used to estimate a Km for an enzymatic reaction? select all that apply 2. Which graph(s) can be used to calculate an association constant for a protein binding its ligand? select all that apply 3. Which graph(s) can be used to estimate protein stability and to understand folding thermodynamics? select all that apply 4. Which graph(s) can be used to estimate the equilibrium constant for the dissociation of a protein-ligand complex? select all that apply...