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![- In this km is unchanged and Umax is lowered. when when inhibitor is used Vmax Vmax - km [s] Lineweaver Burk plot](http://img.homeworklib.com/questions/2ae33220-eced-11ea-9316-154a1a2112e7.png?x-oss-process=image/resize,w_560)
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c. Describe the properties of i, competitive inhibitor and ii, noncompetitive inhibitor for this enzyme. Draw...
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.
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.
aOn a Lineweaer-Burk plot for a competitive inhibitor, the plots for separaterments at different inhabitor will...
aOn a Lineweaer-Burk plot for a competitive inhibitor, the plots for separaterments at different inhabitor will intersect on the 1/Waxis Correct A competitive inhibitor will alter the apparent Kyof an enzyme-substrate combination but will not alter the apparent ax Value. On a Lineweaver-Burk plot for a competitive inhibitor, the plots for separate experiments at different inhibitor concentrations will intersect on the 1/Waxis. The intersection will be at the point Choose one 0 1/[sj = 1 KM and 1,7:0 O 1/[S]...
The inhibitor Draw a sketch on where a(n). inhibitor binds to the enzyme: The reaction in...
The inhibitor Draw a sketch on where a(n). inhibitor binds to the enzyme: The reaction in the presence of a(n)inhibitor can be written In the Michaelis-Menten graph, the inhibited reaćtion would look this as compared tot he uninhibited reaction (label both axes and draw both curves). In the Lineweaver-Burk graph, the inhibited reaction would look like this as compared tot he uninhibited reaction (label both axes and draw both curves). inhibitor, the apparent changes of Vmax and Km are as...
For a report, after plotting the lineweaver-burk plot for a protease enzyme with and without inhibitor....
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.
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
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
show work please! with inhibitor (umoles/min/mg) [S] (mm) v- no inhibitor (umoles/min/mg) V - with inhibitor...
show work please!
with inhibitor (umoles/min/mg) [S] (mm) v- no inhibitor (umoles/min/mg) V - with inhibitor (umoles 3.0 2.29 x 103 1.83 x 103 5.0 or ble 3.20 x 103 Boristeder s obre o 2.56 x 103 7.0 3.86 x 103 USD 3.09 x 103 0 9. 4 .36 x 100W 3.49 x 103 0 11. 4 .75 x 108 3.80 x 103 Draw Lineweaver-Burk plots for the enzyme data shown above. When present, I = 0.200 m a) What...
An enzyme-catalyzed reaction to the presence of 5 nM of reversible inhibitor yields a Vmax value...
An enzyme-catalyzed reaction to the presence of 5 nM of reversible inhibitor yields a Vmax value that is 80% of the value in absence of the inhibitor. The KMvalue is unchanged. a) what type of inhibition is occurring? b) what proportion of the enzyme molecule will have bound inhibitor? c) Draw the Lineweaver-Burk (known as double-reciprocal plot) for uninhibited and inhibited reaction. SHOW ALL YOUR WORK PLEASE
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]...
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.
aOn a Lineweaer-Burk plot for a competitive inhibitor, the plots for separaterments at different inhabitor will intersect on the 1/Waxis Correct A competitive inhibitor will alter the apparent Kyof an enzyme-substrate combination but will not alter the apparent ax Value. On a Lineweaver-Burk plot for a competitive inhibitor, the plots for separate experiments at different inhibitor concentrations will intersect on the 1/Waxis. The intersection will be at the point Choose one 0 1/[sj = 1 KM and 1,7:0 O 1/[S]...
The inhibitor Draw a sketch on where a(n). inhibitor binds to the enzyme: The reaction in the presence of a(n)inhibitor can be written In the Michaelis-Menten graph, the inhibited reaćtion would look this as compared tot he uninhibited reaction (label both axes and draw both curves). In the Lineweaver-Burk graph, the inhibited reaction would look like this as compared tot he uninhibited reaction (label both axes and draw both curves). inhibitor, the apparent changes of Vmax and Km are as...
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
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
show work please!
with inhibitor (umoles/min/mg) [S] (mm) v- no inhibitor (umoles/min/mg) V - with inhibitor (umoles 3.0 2.29 x 103 1.83 x 103 5.0 or ble 3.20 x 103 Boristeder s obre o 2.56 x 103 7.0 3.86 x 103 USD 3.09 x 103 0 9. 4 .36 x 100W 3.49 x 103 0 11. 4 .75 x 108 3.80 x 103 Draw Lineweaver-Burk plots for the enzyme data shown above. When present, I = 0.200 m a) What...
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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