![2. a) The Michaelis-Menten mechanism is +KTERE] - @s→Es (rateco nstant kl) ク ES→ E + S (rate constant k2) E S ES-XⓟHE) orate constant k3) So d[PVdt- k3[ES] Use the steady state approximation to show [El/[ES] (k2+k3)/(k1[S] b) let Km=(k2+k3)/kl and show that you get the expression ·J [EVIES]-Km/[S] c) We will talk in class about how this information eventually gives rise the expression d[P]/dt-k3E][S/(Km +IS) Usually [S>>Km. Show what this equation simplifies to in this case This is defined as Vmax d) Rewrite equation I using Vmax instead so your expression should now look like rate-Vmax[S(Km+[S]) e) A Lineweaver Burk plot is a graph of I/rate (y-axis) vs. 1/[S] (x-axis). Based on the equation from part d), show what the slope and intercept of a Lineweaver-Burk plot will be. 4. A possible mechanism for the decomposition of ozone in the reaction 203 (g) → 3。2(g) is: ana uie dennst end with a) The intermediate in this reaction is](http://img.homeworklib.com/questions/cd9f3d20-7cc4-11eb-88c1-b59c58041b93.png?x-oss-process=image/resize,w_560)
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how we can solve q2
2. a) The Michaelis-Menten mechanism is +KTERE] - @s→Es (rateco nstant...
Consider the following modification of the Michaelis Menten mechanism: E + S ES rightarrow E +...
Consider the following modification of the Michaelis Menten mechanism: E + S ES rightarrow E + P E + I EI In this mechanism, a second molecule. I, can bind to the free enzyme and prevent (or compete with) the binding of substrate. If the [S] is much greater than [I], would you expect the velocity (d[P]/dt) for this mechanism to be different than for the Michaelis Menton mechanism? Draw- a Lineweaver Burk plot for this mechanism. The first line...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is give...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the...
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the initial velocity, Vo, of an enzymatic reaction and substrate concentration, [S]. There are three conditions that are useful for simplifying the Michaelis-Menten equation: [S] <<Km; [S] = Km; [S] >> Km. Match each condition with the statement(s) that describe it. TV, Vmox[S] Vo =Vmax m . V Vo - Vmax [S] Km +[S] V. (um/min) max [S] (mm) (a) Doubling [S] will almost double...
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...
michaelis menten and kinetics help 2. A few years after Michaelis Menten published their work Briggs and Haldane came along and expanded it using the steady state assumption. i) Based on kinetic s...
michaelis menten and kinetics help
2. A few years after Michaelis Menten published their work Briggs and Haldane came along and expanded it using the steady state assumption. i) Based on kinetic scheme 2 how many different ways can ES be produced? i) Using the rate constants in kinetic Scheme 2 at what rate is the ES complex being produced? sed eci iv) Using the rate constants in kinetic Scheme 2 at what rate is the ES complex being destroyed?...
Quest. 3 (10 pts). Examine the following mechanism Step 1 2N2O2(g) Step 2 2N2O(g) + 2H2...
Quest. 3 (10 pts). Examine the following mechanism Step 1 2N2O2(g) Step 2 2N2O(g) + 2H2 (g) → → 2N2O(g) + O2(g) 2N2 (g) + 2H2O(g) (kl; slow) (k2; fast) a) (2 pts) Write the overall equation for the reaction. b) (2 pts) Identify the intermediate(s) and/or catalyst(s) if any. c) (2 pts) Write the rate law for the overall reaction. d) (1 pts) State the order of the reaction e) (2 pts) Write the integrated rate equation f) (1...
C370S19HW3 Name Please attach your plots to this sheet and turn in your work on Monday June 3 The enzyme urease...
C370S19HW3 Name Please attach your plots to this sheet and turn in your work on Monday June 3 The enzyme urease catalyzes the hydrolysis of urea. 1. (3) Write the reaction catalyzed by Urea below: 2. (2) Of the 7 classes of Enzymes, which type is urease? 3. The rate of this reaction was determined for a series of solutions in which the concentration of urea was changed while maintaining a fixed urease concentration of 3.0 HM. The following data...
2. hypothesize the best conditions (pH and temperature) under which the enzyme chymotrypsin functions with an...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
Based on the document below, 1. Describe the hypothesis Chaudhuri et al ids attempting to evaluate;...
Based on the document below,
1. Describe the hypothesis Chaudhuri et al ids attempting to
evaluate; in other words, what is the goal of this paper? Why is he
writing it?
2. Does the data presented in the paper support the hypothesis
stated in the introduction? Explain.
3.According to Chaudhuri, what is the potential role of thew
alkaline phosphatase in the cleanup of industrial waste.
CHAUDHURI et al: KINETIC BEHAVIOUR OF CALF INTESTINAL ALP WITH PNPP 8.5, 9, 9.5, 10,...
I need Summary of this Paper i dont need long summary i need What methodology they used , what is the purpose of this p...
I need Summary of this Paper i dont need long summary i need
What methodology they used , what is the purpose of this paper and
some conclusions and contributes of this paper. I need this for my
Finishing Project so i need this ASAP please ( IN 1-2-3 HOURS
PLEASE !!!)
Budgetary Policy and Economic Growth Errol D'Souza The share of capital expenditures in government expenditures has been slipping and the tax reforms have not yet improved the income...
Consider the following modification of the Michaelis Menten mechanism: E + S ES rightarrow E + P E + I EI In this mechanism, a second molecule. I, can bind to the free enzyme and prevent (or compete with) the binding of substrate. If the [S] is much greater than [I], would you expect the velocity (d[P]/dt) for this mechanism to be different than for the Michaelis Menton mechanism? Draw- a Lineweaver Burk plot for this mechanism. The first line...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the initial velocity, Vo, of an enzymatic reaction and substrate concentration, [S]. There are three conditions that are useful for simplifying the Michaelis-Menten equation: [S] <<Km; [S] = Km; [S] >> Km. Match each condition with the statement(s) that describe it. TV, Vmox[S] Vo =Vmax m . V Vo - Vmax [S] Km +[S] V. (um/min) max [S] (mm) (a) Doubling [S] will almost double...
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...
michaelis menten and kinetics help
2. A few years after Michaelis Menten published their work Briggs and Haldane came along and expanded it using the steady state assumption. i) Based on kinetic scheme 2 how many different ways can ES be produced? i) Using the rate constants in kinetic Scheme 2 at what rate is the ES complex being produced? sed eci iv) Using the rate constants in kinetic Scheme 2 at what rate is the ES complex being destroyed?...
Quest. 3 (10 pts). Examine the following mechanism Step 1 2N2O2(g) Step 2 2N2O(g) + 2H2 (g) → → 2N2O(g) + O2(g) 2N2 (g) + 2H2O(g) (kl; slow) (k2; fast) a) (2 pts) Write the overall equation for the reaction. b) (2 pts) Identify the intermediate(s) and/or catalyst(s) if any. c) (2 pts) Write the rate law for the overall reaction. d) (1 pts) State the order of the reaction e) (2 pts) Write the integrated rate equation f) (1...
C370S19HW3 Name Please attach your plots to this sheet and turn in your work on Monday June 3 The enzyme urease catalyzes the hydrolysis of urea. 1. (3) Write the reaction catalyzed by Urea below: 2. (2) Of the 7 classes of Enzymes, which type is urease? 3. The rate of this reaction was determined for a series of solutions in which the concentration of urea was changed while maintaining a fixed urease concentration of 3.0 HM. The following data...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
Based on the document below,
1. Describe the hypothesis Chaudhuri et al ids attempting to
evaluate; in other words, what is the goal of this paper? Why is he
writing it?
2. Does the data presented in the paper support the hypothesis
stated in the introduction? Explain.
3.According to Chaudhuri, what is the potential role of thew
alkaline phosphatase in the cleanup of industrial waste.
CHAUDHURI et al: KINETIC BEHAVIOUR OF CALF INTESTINAL ALP WITH PNPP 8.5, 9, 9.5, 10,...
I need Summary of this Paper i dont need long summary i need
What methodology they used , what is the purpose of this paper and
some conclusions and contributes of this paper. I need this for my
Finishing Project so i need this ASAP please ( IN 1-2-3 HOURS
PLEASE !!!)
Budgetary Policy and Economic Growth Errol D'Souza The share of capital expenditures in government expenditures has been slipping and the tax reforms have not yet improved the income...
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