Draw a plot of 1/[v_0] vs 1/[s] for a Michaelis-Menton enzymatic reaction in the presence of...
Draw a plot of 1/[v_0] vs 1/[s] for a Michaelis-Menton enzymatic reaction in the presence of different concentrations of an uncompetitive inhibitor. Label all intercepts, slopes, axis, V_max, Km,KI, and I. Please explain your diagram.
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Draw a plot of 1/[v_0] vs 1/[s] for a Michaelis-Menton enzymatic
reaction in the presence of...
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as...
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...
The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme...
The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme (E) that catalyzes the hydrolysis of a peptide substrate (S). All data were generated in the presence of 18.0 μM total enzyme. The enzyme-catalyzed reaction has a Km of 3.00 μM and a Vmax of 2.00 μM/sec. The enzyme-catalyzed reaction in the presence of 15.0 μM of Inhibitor A has an apparent Km of 2.25 μM and an apparent Vmax of 1.50 μM/sec. The...
Where do the numbers come from for a Michaelis-Menton and Lineweaver-Burke Plot? Can you please explain...
Where do the numbers come from for a Michaelis-Menton and
Lineweaver-Burke Plot? Can you please explain in detail please and
thank you?
Did
an Enzyme lab w/dilutions and recorded absorbances. I am now asked
to construct Michaelis-Menton ans Lineweaver-Burke plots BUT I dont
know if the plot is based on my results from the dilutions and
absorbances.
For your lab reports, you will determine how much sugar was made during your enzyme reactions in Week 2 based on the linear...
ISU Question 3: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]....
ISU Question 3: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo 1/[S1 1/V0 UM (UM/s) M (s/uM) 340 10 2.94E-03 0.2 530 740 0.8 910 1.6 1040 0.4 a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest (SD? c) Using your Vmax estimate, calculate 14 Vmax, and using your curve, estimate Km....
The table below lists initial velocities measured for an enzymatic reaction at different substrate concentrations in...
The table below lists initial velocities measured for an enzymatic reaction at different substrate concentrations in the presence and absence of an inhibitor. The enzyme concentration is identical in both reactions. Graph a Lineweaver-Burk plot. What are the apparent values of vmax and km for each experiment? what is the inhibition mechanism If the concentration of inhibitor is 0.5 mM, what is the value of K1?
Please do everything like you were answering a test. Don’t attempt if youre not going to do all p...
Please do everything like you were answering a test. Don’t attempt
if youre not going to do all parts. Do it ASAP and I will give you
a good rating. If not I will report you. Thank you so much for
being the best. Show work if necessary and be concise. There’s no
way for me to separate so do all parts.
do all parts please. I cant seperate it because it will be
refunded.
2. i) (10 points) The...
Please answer all of those questions 7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bo...
Please answer all of those questions
7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...
21 and 22 please with work shown 21/ Show that for competitive inhibition of an enzymatic...
21 and 22 please with work shown
21/ Show that for competitive inhibition of an enzymatic reaction, the intercepts on the horizontal axis of a plot of 1/v versus 1/[S) at different inhibitor concentrations are equal to 1/Km (1 + [/K). 48 81 73 0.4 145 (22 [S] (UM) y - no inhibitor (um/min) y - with inhibitor (UM/min) Ti g t be 0.1 0.2 123 wool 0.6 95 0.75 160 108 Renin acts as a specific protease that cleaves...
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equatio...
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equation as shown below: V0 = (-Km) V0 / [S] + Vmax a). Please derive the Eadie-Hofstee equation starting from the Michaelis-Menten equation. b). The Vmax and Km of the enzyme catalyzed reaction can be derived from a plot of V0 versus V0/[S]. Please draw one of these plots and explain how do you use it to derive Vmax and Km. c). Please draw a...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence and absence of 3 mM inhibitor Z. The initial velocity data obtained are shown below: [S] (mmoles liter) v (mmoles"litermin) no inhibitor inhibitor Z 1.25 1.67 2.50 5.00 10.0 1.72 2.04 2.63 3.33 4.17 0.98 1.17 1.47 1.96 2.38 (4 pts) Estimat e Vmax and Kw in the presence and absence of inhibitor using the Michaelis Menton curve-fitting program on Kaleidagraph (see lab manual)....
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...
Where do the numbers come from for a Michaelis-Menton and
Lineweaver-Burke Plot? Can you please explain in detail please and
thank you?
Did
an Enzyme lab w/dilutions and recorded absorbances. I am now asked
to construct Michaelis-Menton ans Lineweaver-Burke plots BUT I dont
know if the plot is based on my results from the dilutions and
absorbances.
For your lab reports, you will determine how much sugar was made during your enzyme reactions in Week 2 based on the linear...
ISU Question 3: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo 1/[S1 1/V0 UM (UM/s) M (s/uM) 340 10 2.94E-03 0.2 530 740 0.8 910 1.6 1040 0.4 a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest (SD? c) Using your Vmax estimate, calculate 14 Vmax, and using your curve, estimate Km....
The table below lists initial velocities measured for an enzymatic reaction at different substrate concentrations in the presence and absence of an inhibitor. The enzyme concentration is identical in both reactions. Graph a Lineweaver-Burk plot. What are the apparent values of vmax and km for each experiment? what is the inhibition mechanism If the concentration of inhibitor is 0.5 mM, what is the value of K1?
Please do everything like you were answering a test. Don’t attempt
if youre not going to do all parts. Do it ASAP and I will give you
a good rating. If not I will report you. Thank you so much for
being the best. Show work if necessary and be concise. There’s no
way for me to separate so do all parts.
do all parts please. I cant seperate it because it will be
refunded.
2. i) (10 points) The...
Please answer all of those questions
7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...
21 and 22 please with work shown
21/ Show that for competitive inhibition of an enzymatic reaction, the intercepts on the horizontal axis of a plot of 1/v versus 1/[S) at different inhibitor concentrations are equal to 1/Km (1 + [/K). 48 81 73 0.4 145 (22 [S] (UM) y - no inhibitor (um/min) y - with inhibitor (UM/min) Ti g t be 0.1 0.2 123 wool 0.6 95 0.75 160 108 Renin acts as a specific protease that cleaves...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence and absence of 3 mM inhibitor Z. The initial velocity data obtained are shown below: [S] (mmoles liter) v (mmoles"litermin) no inhibitor inhibitor Z 1.25 1.67 2.50 5.00 10.0 1.72 2.04 2.63 3.33 4.17 0.98 1.17 1.47 1.96 2.38 (4 pts) Estimat e Vmax and Kw in the presence and absence of inhibitor using the Michaelis Menton curve-fitting program on Kaleidagraph (see lab manual)....
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