Consider an enzyme catalyzed reaction taking place in an aqueous solution. If the earlier process of folding the enzyme results in a large decrease in the entropy of the system, how would this impact the rate of the catalyzed reaction.
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Consider an enzyme catalyzed reaction taking place in an aqueous solution. If the earlier process of folding the enzyme results in a large decrease in the entropy of the system, how would this impact the rate of the catalyzed reaction.
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- Would you expect an “enzyme” designed to bind its target substrate as tightly as it binds the reaction transition state to show a rate enhancement over the uncatalyzed reaction? In other words, would such protein be a catalyst? Use a reaction energy diagram to explain why or why not.Show graphically how the reaction velocity depends on the enzyme concentration. Can a reaction be saturated with enzyme?The figure displays the relationship between initial rate of product formation and reactant concentration in an enzyme-catalyzed reaction with a fixed amount of enzyme. Which of the following statements best explains the shape of the rate curve at high reactant concentration?
- Consider the analogy of the jiggling box containing coins that was described on page 85. The reaction, the flipping of coins that either face heads up (h) or tails up (T), is described by the equation h ↔ T, where the rate of the forward reaction equals the rate of the reverse reaction.a. What are ΔG and ΔG° in this analogy? b. What corresponds to the temperature at which the reaction proceeds? What corresponds to the activation energy of the reaction? assume you have an “enzyme,” called jigglase, which catalyzes this reaction. What would the effect of jigglase be and what, mechanically, might jigglase do in this analogy?In terms of potential and kinetic energy where does the energy comes from that allows an enzyme to lower the activation energy of a reaction? Is thermal energy involved?Students conducting research observe the rate of an enzyme-catalyzed reaction under various conditions with a fixed amount of enzyme in each sample. When will increasing the substrate concentration likely result in the greatest increase in the reaction rate?
- Which of the following statements helps best explain the reaction specificity of an enzyme? a) The shape and charge of the substrates are compatible with the active site of the enzyme. b) The free energy of the reactants is greater than the free energy of the products. c) The equilibrium constant of the reaction is much greater than 1. d) The concentration of the enzyme inside living cells is greater than the concentration of substrate.Draw and label the rate law graph for an allosteric enzyme? Give an explanation for the shape of the curve.We can increase the rate of a reaction by decreasing the activation energy. And, we can do it by using an enzyme. Explain how enzyme decrease the activation energy.
- Which of the following would best explain how an enzyme catalyzes two different reactions? A) The enzyme contains a-helices and B-pleated sheets. B) The enzyme is subject to cooperativity C) Either the enzyme has two distinct active sites or the substrates involved in the two reactions have very similar structures D) The enzyme is subject to competitive inhibition and allosteric regulation E) The enzyme is composed of at least two subunitsGraph a double reciprocal plot that satisfy the following: a. Michaelis-Menten kinetics enzyme, b. an inhibitor that binds only free enzyme (competitive), c. an inhibitor that binds only enzyme-substrate complex.In enzyme kinetics, why are measurements made at the start of a reaction?