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6X 10+ 200 3. What concentration of competitive inhibitor is required to yield 75% inhibition at...
a) What concentration of competitive inhibitor is required to yield 75% inhibition at a substrate concentration...
a) What concentration of competitive inhibitor is required to yield 75% inhibition at a substrate concentration of 1.5x10-3 M if Km=2.9x10-4 and Ki=2x10-5? b)To what concentration must the substrate be increased to re-establish the velocity at the original uninhibited value?
26. In a competitive inhibitor experiment, measured KM without inhibitor is 75 nM. After additing 3...
26. In a competitive inhibitor experiment, measured KM without inhibitor is 75 nM. After additing 3 M of inhibitor, the new Km is 225 nM. What is the closest value of a for the inhibition in this reaction? a. 1 b. 2 c. 3 d. 9 27. In the Question 26, what is the Ki for this inhibitor? a. 0.3 nM b. 0.75 nM c. 1.5 nM d. 3.0 nM 28. Which of the following about metabolism is INCORRECT?
An enzyme binds to a competitive inhibitor with Kd = 1.2 × 10-6 M at pH 7.0 and 25°C.
An enzyme binds to a competitive inhibitor with Kd = 1.2 × 10-6 M at pH 7.0 and 25°C.(a)At what inhibitor concentration will 75% of the enzyme be bound to the inhibitor if there is no substrate present? (b) This enzyme has a Km of 4.0 × 10-5 M and a Vmax of 50 μM/s. At a substrate concentration of 3.0 × 10-4 M, calculate (i) the velocity of reaction in the presence of the inhibitor at 4.8 x 10-5 M (ii) the degree of...
A compound is a strong competitive inhibitor with an a = 10. The total enzyme concentration...
A compound is a strong competitive inhibitor with an a = 10. The total enzyme concentration in the reaction is 10 nM. What substrate concentration reduces the velocity to 250 nM/min, knowing that this enzyme is characterized by a specificity constant of 2.1 x 105 M-1s-1 and a kcat of 25/min?
a. what are the values of Vmax and Km in the abscence if the inhibitor what...
a. what are the values of Vmax and Km in the abscence if the
inhibitor what are the values of Vmax and Km in the presence of the
inhibitor?
b. what type of inhibition is it?
c. what is the dissociation constant (Ki) of the
inhibition?
***d. graph a linear scatter plot including equation.
Homework (CHE 407) The initial velocity for an enzyme-catalyzed reaction is measured at various initial substrate concentration [S]o, in the absence and in the presence of...
Problem Set #3 Due in class 10/10/18 se in a classic 1. Sucrose (common table sugar)...
Problem Set #3 Due in class 10/10/18 se in a classic 1. Sucrose (common table sugar) is hydrolyzed to glucose and fructo experiment in kinetics. The reaction is catalyzed by the enzyme invertase. Using the following data, determine by the Lineweaver-Burke method A) the Vmax and Km of the enzyme and B) whether the inhibition of this reaction by 2 M urea is competitive or noncompetitive. V, no inhibitor (arbitrary units) V, inhibitor present (same arbitrary units) Sucrose concentration 0.0292...
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,...
will work with up to 3 partners (similar to a lab group) to prepare a written report which analyzes kinetic data that has been provided to you. All student groups will receive data for the hy...
will work with up to 3 partners (similar to a lab group) to prepare a written report which analyzes kinetic data that has been provided to you. All student groups will receive data for the hypothetical reaction aAlE) products where a is a numeric variable and A is a chemical variable. The reaction therefore has the form of a decomposition reaction, in which a single substance forms one or more new substances. For consistency, all concentrations start out at 1.000...
1) What chemical is the titrant in this experiment? What chemical is the analyte in this experiment? Experi...
1) What chemical is the titrant in this experiment? What
chemical is the analyte in this
experiment?
Experiment #8: Measuring the Vitamin C Content of Emergen-C™ Objectives: • Students will learn how to use a burette. • Students will learn how to use the iodine starch indicator system to monitor oxidation/reduction reactions. Students will learn how to conduct a titration to determine the amount of analyte in an unknown solution. • Students will learn about ascorbic acid's role as a...
1. According to the paper, what does lactate dehydrogenase (LDH) do and what does it allow...
1. According to the paper, what does lactate dehydrogenase
(LDH) do and what does it allow to happen within the myofiber? (5
points)
2. According to the paper, what is the major disadvantage of
relying on glycolysis during high-intensity exercise? (5
points)
3. Using Figure 1 in the paper, briefly describe the different
sources of ATP production at 50% versus 90% AND explain whether you
believe this depiction of ATP production applies to a Type IIX
myofiber in a human....
26. In a competitive inhibitor experiment, measured KM without inhibitor is 75 nM. After additing 3 M of inhibitor, the new Km is 225 nM. What is the closest value of a for the inhibition in this reaction? a. 1 b. 2 c. 3 d. 9 27. In the Question 26, what is the Ki for this inhibitor? a. 0.3 nM b. 0.75 nM c. 1.5 nM d. 3.0 nM 28. Which of the following about metabolism is INCORRECT?
a. what are the values of Vmax and Km in the abscence if the
inhibitor what are the values of Vmax and Km in the presence of the
inhibitor?
b. what type of inhibition is it?
c. what is the dissociation constant (Ki) of the
inhibition?
***d. graph a linear scatter plot including equation.
Homework (CHE 407) The initial velocity for an enzyme-catalyzed reaction is measured at various initial substrate concentration [S]o, in the absence and in the presence of...
Problem Set #3 Due in class 10/10/18 se in a classic 1. Sucrose (common table sugar) is hydrolyzed to glucose and fructo experiment in kinetics. The reaction is catalyzed by the enzyme invertase. Using the following data, determine by the Lineweaver-Burke method A) the Vmax and Km of the enzyme and B) whether the inhibition of this reaction by 2 M urea is competitive or noncompetitive. V, no inhibitor (arbitrary units) V, inhibitor present (same arbitrary units) Sucrose concentration 0.0292...
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,...
will work with up to 3 partners (similar to a lab group) to prepare a written report which analyzes kinetic data that has been provided to you. All student groups will receive data for the hypothetical reaction aAlE) products where a is a numeric variable and A is a chemical variable. The reaction therefore has the form of a decomposition reaction, in which a single substance forms one or more new substances. For consistency, all concentrations start out at 1.000...
1) What chemical is the titrant in this experiment? What
chemical is the analyte in this
experiment?
Experiment #8: Measuring the Vitamin C Content of Emergen-C™ Objectives: • Students will learn how to use a burette. • Students will learn how to use the iodine starch indicator system to monitor oxidation/reduction reactions. Students will learn how to conduct a titration to determine the amount of analyte in an unknown solution. • Students will learn about ascorbic acid's role as a...
1. According to the paper, what does lactate dehydrogenase
(LDH) do and what does it allow to happen within the myofiber? (5
points)
2. According to the paper, what is the major disadvantage of
relying on glycolysis during high-intensity exercise? (5
points)
3. Using Figure 1 in the paper, briefly describe the different
sources of ATP production at 50% versus 90% AND explain whether you
believe this depiction of ATP production applies to a Type IIX
myofiber in a human....
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