Homework Answers
13. 
The magnitude of
ΔGact increases by the virtue of the new E.S being lower
in energy (because it is more stable).
14.
The magnitude of ΔGact further increases because the enzyme is more tightly bound to the substrate and hence E.S is lowered more in energy.
Add Answer to:
13. Suppose a second enzyme binds the substrate even more tightly than the enzyme shown in model 1 (the ES complex...
Reset Help complexEnzymes catalyze reaction by stabilizing the If the enzyme binds to the substrate too...
Reset Help complexEnzymes catalyze reaction by stabilizing the If the enzyme binds to the substrate too Thus, the enzyme binds best to induced fit lock and key transition state well, the activation energy for the catalyzed reaction the and the activation energy In the model, the enzyme binds to the most efficiently decreases In the model, both the enzyme and change their structure upon remains about the same binding in a way that favors the formation of the increases Thus,...
10. A good transition-state analog: A) binds covalently to the enzyme. B) binds to the enzyme...
10. A good transition-state analog: A) binds covalently to the enzyme. B) binds to the enzyme more tightly than the substrate. C) binds very weakly to the enzyme. D) is too unstable to isolate. E) must be almost identical to the substrate. 11. Which factor bas NOT been shown to play a role in determining the specificity of protein kinases? A) disulfide bonds near the phosphorylation site B) primary sequence at phosphorylation site C) protein quaternary structure D) protein tertiary...
Uncatalyzed Catalyzed Enzyme-substrate Complex In the above reaction, the lower curve is an enzyme-catalyzed reaction where...
Uncatalyzed Catalyzed Enzyme-substrate Complex In the above reaction, the lower curve is an enzyme-catalyzed reaction where the activation energy is notably lower than the uncatalyzed reaction. Suppose the enzyme in the diagram was mutated in such a way that its affinity for the substrate increased 100 fold, thereby affecting the enzyme-substrate complex portion of the curve. Assume that there was no other effect. Would you expect the reaction rate catalyzed by the altered enzyme to be faster, slower, or equal...
questions 7-11 emists, E + S and E. S have very specific meanings. Describe the differences...
questions 7-11
emists, E + S and E. S have very specific meanings. Describe the differences as concisely as possible. According to the graphs, which is more stable? How do you know Label the difference in free energy between E + S and E.S on your graph as "AGES Describe what E+S* (on graph A) and E.S+ (on graph B) mean. Which is 10. Label this difference in free energy between E + St and E.St on the graphs as...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much of their three dimensional shape is the result of interactions between the R (variable) groups of their amino acids. The active site is the portion of the enzyme that will interact with the substrate the molecule that the enzyme acts upon. The nature and arrangement of amino acids in the active site make each enzyme specific to a substrate and to the reaction it...
Model 1 - Potential Energy Diagrams 1) The energy (enthalpy) change of a reaction can be...
Model 1 - Potential Energy Diagrams 1) The energy (enthalpy) change of a reaction can be determined by the following expression: Activated Complex Transition State AH = Energy products - Energy reactants Activation Energy, E Reactants Consider the energy change for the reaction in Model 1 (the graph to the left). Potential Energy (kJ/mol) Energy change (AH) Products a) The energy change shown is (positive/negative). b) This reaction is (endothermic / exothermic). c) These (reactants / transition state) has more...
I answered E but I cannot figure out part F? Using your value from the previous...
I answered E but I cannot figure out part F?
Using your value from the previous question, determine how many
H bonds or dipole interactions would be required to achieve a rate
enhancement of 10^6.
Part E A rate enhancement of 100 requires that the enzyme bind its transition state complex with higher affinity than its substrate. Using the Arrhenius equation, shown before this part, find AAGEat for a rate enhancement of 106 at 298 K. Express AAGEat in kJ/mol...
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,...
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....
Reset Help complexEnzymes catalyze reaction by stabilizing the If the enzyme binds to the substrate too Thus, the enzyme binds best to induced fit lock and key transition state well, the activation energy for the catalyzed reaction the and the activation energy In the model, the enzyme binds to the most efficiently decreases In the model, both the enzyme and change their structure upon remains about the same binding in a way that favors the formation of the increases Thus,...
10. A good transition-state analog: A) binds covalently to the enzyme. B) binds to the enzyme more tightly than the substrate. C) binds very weakly to the enzyme. D) is too unstable to isolate. E) must be almost identical to the substrate. 11. Which factor bas NOT been shown to play a role in determining the specificity of protein kinases? A) disulfide bonds near the phosphorylation site B) primary sequence at phosphorylation site C) protein quaternary structure D) protein tertiary...
Uncatalyzed Catalyzed Enzyme-substrate Complex In the above reaction, the lower curve is an enzyme-catalyzed reaction where the activation energy is notably lower than the uncatalyzed reaction. Suppose the enzyme in the diagram was mutated in such a way that its affinity for the substrate increased 100 fold, thereby affecting the enzyme-substrate complex portion of the curve. Assume that there was no other effect. Would you expect the reaction rate catalyzed by the altered enzyme to be faster, slower, or equal...
questions 7-11
emists, E + S and E. S have very specific meanings. Describe the differences as concisely as possible. According to the graphs, which is more stable? How do you know Label the difference in free energy between E + S and E.S on your graph as "AGES Describe what E+S* (on graph A) and E.S+ (on graph B) mean. Which is 10. Label this difference in free energy between E + St and E.St on the graphs as...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much of their three dimensional shape is the result of interactions between the R (variable) groups of their amino acids. The active site is the portion of the enzyme that will interact with the substrate the molecule that the enzyme acts upon. The nature and arrangement of amino acids in the active site make each enzyme specific to a substrate and to the reaction it...
Model 1 - Potential Energy Diagrams 1) The energy (enthalpy) change of a reaction can be determined by the following expression: Activated Complex Transition State AH = Energy products - Energy reactants Activation Energy, E Reactants Consider the energy change for the reaction in Model 1 (the graph to the left). Potential Energy (kJ/mol) Energy change (AH) Products a) The energy change shown is (positive/negative). b) This reaction is (endothermic / exothermic). c) These (reactants / transition state) has more...
I answered E but I cannot figure out part F?
Using your value from the previous question, determine how many
H bonds or dipole interactions would be required to achieve a rate
enhancement of 10^6.
Part E A rate enhancement of 100 requires that the enzyme bind its transition state complex with higher affinity than its substrate. Using the Arrhenius equation, shown before this part, find AAGEat for a rate enhancement of 106 at 298 K. Express AAGEat in kJ/mol...
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,...
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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