Homework Answers
In competitive inhibitor Km increases to apparent higher value and Vmax remains constant with addition of inhibitor.
In non competitive inhibitor Km remains constant and Vmax decreases with addition of inhibitor
In mixed inhibitor Km increases or decrease and Vmax decreases with addition of inhibitor.
Therefore, for above reaction inhibition is competitive.
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21. When you measure an enzyme reaction both without and with several concentrations of an inhibitor,...
You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD...
You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD Previously, you determined that kcat = 400 s and Km = 10 M for your sample of happyase. Further research shows that this happyase sample was actually contaminated with a reversible inhibitor called ANGER. When ANGER is fully removed from the happyase preparation and [Eltotalis 4 nM, the measured Vmax is increased to 4.8 umes-1 and the measured Km is now 15 MM. Use...
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.
Question 14 What is the approximate Keq for this reaction? GTP+TDP → GDP+TTP near 1 0...
Question 14 What is the approximate Keq for this reaction? GTP+TDP → GDP+TTP near 1 0 -1 Not enough information was given. Question 15 What is the approximate ∆G'° for this reaction? GTP+TDP → GDP+TTP Near 0 Near 1 Near -1 Not enough information was given. Question 16 Succinate dehydrogenase, a critical enzyme in the tricarboxylic acid cycle. You are characterizing the possible inhibitor malonate and want to determine its mode of binding to succinate dehydrogenase. Equilibrium dialysis measurements at...
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...
1 2 3 4 5 6 7 8 9 Part A Which of the following is/are...
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2
3
4
5
6
7
8
9
Part A Which of the following is/are means whereby a catalyst can lower the activation energy of a reaction? quantum tunneling decreasing the number of reactive molecules permanently binding substrates inefficient collisions altering the temperature within the cell to one appropriate for reactions to proceed Subrnit Request Answer Part A An enzyme Obinds substrates in a manner that facilitates the formation of product decreases the rate of a reaction. is always...
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,...
Can't figure out the concentration of the complex of solns. 10, 11, 12, 13, & 14. Modern...
Can't figure out the concentration of the complex of
solns. 10, 11, 12, 13, & 14.
Modern Experimental Chemistry Chemistry 153 The Iron(III) Thiocyanate Complex Purpose of the Experiment To determine the chemical formula of a complex ion and measure its formation equilibrium constant Equipment Spectro Vis spectrophotometer and LabQuest, cuvette, 25-mL buret (3), ring stand, buret clamp (2), 50-mL beaker (3), small plastic beakers Reagents SCN, as KSCN, 0.00200 M solution Fe; as Fe(NO), 0.00200 M solution and a...
just one example/demonstration! Data needed to be calculated is in highlighted in green boxes. And I...
just one example/demonstration!
Data needed to be calculated is in highlighted in green boxes.
And I highlighted in red an equation (not sure if thats what you
use to calculate it) And ignore the lab instructions on completeing
a graph!! I already know how to do that in excel, just curious how
Ln (relative rate) and 1/T in K^-1 is calculated by hand*
here is the rest of that lab leading up to the question as I
know its typically...
Separating a Mixture, Recrystallization, pre-lab assignment could you also explain why you chose that substance for...
Separating a Mixture, Recrystallization, pre-lab
assignment
could you also explain why you chose that substance for the empty
spaces and question marks
EXPERIMENT 4 Pre-Lab Assignment Separating a Mixture, Recrystalliration Name Date 1. Complete the following flowchart which shows how to separate a mixture of sand, sodium chloride and acetanilide. Notice that after a separation process (a down arrow) the filtered solids are shown on the left and the filtrate (the liquid) is shown on the right. The terminal step...
Introduction: A manufacturing company that possesses many complexities can be highly challenged when maintaining production goals...
Introduction: A manufacturing company that possesses many complexities can be highly challenged when maintaining production goals and standards in conjunction with a major organizational change. Garment manufacturing is a complex industry for many reasons. The product line is a complex array of styles, seasons, varying life cycles and multidimensional sizing. Many sewn product firms are viewing TQM as the appropriate strategy to meet the double demand of competition and quality; however, many companies are finding sustaining their TQM adoption decision...
You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD Previously, you determined that kcat = 400 s and Km = 10 M for your sample of happyase. Further research shows that this happyase sample was actually contaminated with a reversible inhibitor called ANGER. When ANGER is fully removed from the happyase preparation and [Eltotalis 4 nM, the measured Vmax is increased to 4.8 umes-1 and the measured Km is now 15 MM. Use...
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.
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...
1
2
3
4
5
6
7
8
9
Part A Which of the following is/are means whereby a catalyst can lower the activation energy of a reaction? quantum tunneling decreasing the number of reactive molecules permanently binding substrates inefficient collisions altering the temperature within the cell to one appropriate for reactions to proceed Subrnit Request Answer Part A An enzyme Obinds substrates in a manner that facilitates the formation of product decreases the rate of a reaction. is always...
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,...
Can't figure out the concentration of the complex of
solns. 10, 11, 12, 13, & 14.
Modern Experimental Chemistry Chemistry 153 The Iron(III) Thiocyanate Complex Purpose of the Experiment To determine the chemical formula of a complex ion and measure its formation equilibrium constant Equipment Spectro Vis spectrophotometer and LabQuest, cuvette, 25-mL buret (3), ring stand, buret clamp (2), 50-mL beaker (3), small plastic beakers Reagents SCN, as KSCN, 0.00200 M solution Fe; as Fe(NO), 0.00200 M solution and a...
just one example/demonstration!
Data needed to be calculated is in highlighted in green boxes.
And I highlighted in red an equation (not sure if thats what you
use to calculate it) And ignore the lab instructions on completeing
a graph!! I already know how to do that in excel, just curious how
Ln (relative rate) and 1/T in K^-1 is calculated by hand*
here is the rest of that lab leading up to the question as I
know its typically...
Separating a Mixture, Recrystallization, pre-lab
assignment
could you also explain why you chose that substance for the empty
spaces and question marks
EXPERIMENT 4 Pre-Lab Assignment Separating a Mixture, Recrystalliration Name Date 1. Complete the following flowchart which shows how to separate a mixture of sand, sodium chloride and acetanilide. Notice that after a separation process (a down arrow) the filtered solids are shown on the left and the filtrate (the liquid) is shown on the right. The terminal step...
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