Q: Which of the following best describes the relationship between equilibrium and free energy change ($\Delta G$) for a chemical reaction?

At equilibrium, $\Delta G$ is zero and there is no net change in reactant or product concentrations.

Q: A chemical reaction has an activation energy ($E_a$) of 50 kJ/mol and a free energy change ($\Delta G$) of -20 kJ/mol. If the temperature increases, what is the most likely effect on the rate of the reaction?

The rate will increase because more molecules will have enough energy to overcome $E_a$.

Q: Which statement best explains the induced fit model of enzyme function?

The enzyme's active site changes shape to better fit the substrate upon binding, enhancing catalysis.

Q: How does increasing substrate concentration affect the rate of an enzyme-catalyzed reaction, assuming enzyme concentration is constant?

The rate increases and then levels off when the enzyme becomes saturated with substrate.

Q: Which of the following best describes how temperature affects enzyme activity?

Enzyme activity increases with temperature up to an optimal point, then decreases due to denaturation.

Q: A patient is diagnosed with a genetic disorder that results in a non-functional enzyme. Which of the following is the most likely consequence?

The substrate of the enzyme will accumulate, potentially causing toxicity.

Question 1

Which statement best describes the difference between catabolic and anabolic pathways in cellular metabolism?

Accepted Answer

Catabolic pathways break down complex molecules into simpler ones, releasing energy, while anabolic pathways build complex molecules from simpler ones, requiring energy input.

Question 2

Which of the following best summarizes the First Law of Thermodynamics?

Accepted Answer

Energy can be transferred and transformed, but cannot be created or destroyed.

Question 3

Highly ordered living organisms do not violate the Second Law of Thermodynamics because:

Accepted Answer

They increase the entropy of their surroundings by releasing heat and waste, resulting in a net increase in universal entropy.

Question 4

Which of the following reactions is exergonic?

Accepted Answer

A reaction with $\Delta G < 0$ that releases energy.

Question 5

Which of the following best describes the relationship between equilibrium and free energy change ($\Delta G$) for a chemical reaction?

Accepted Answer

At equilibrium, $\Delta G$ is zero and there is no net change in reactant or product concentrations.

Question 6

A chemical reaction has an activation energy ($E_a$) of 50 kJ/mol and a free energy change ($\Delta G$) of -20 kJ/mol. If the temperature increases, what is the most likely effect on the rate of the reaction?

Accepted Answer

The rate will increase because more molecules will have enough energy to overcome $E_a$.

Question 7

Which statement best explains the induced fit model of enzyme function?

Accepted Answer

The enzyme's active site changes shape to better fit the substrate upon binding, enhancing catalysis.

Question 8

How does increasing substrate concentration affect the rate of an enzyme-catalyzed reaction, assuming enzyme concentration is constant?

Accepted Answer

The rate increases and then levels off when the enzyme becomes saturated with substrate.

Question 9

Which of the following best describes how temperature affects enzyme activity?

Accepted Answer

Enzyme activity increases with temperature up to an optimal point, then decreases due to denaturation.

Question 10

A patient is diagnosed with a genetic disorder that results in a non-functional enzyme. Which of the following is the most likely consequence?

Accepted Answer

The substrate of the enzyme will accumulate, potentially causing toxicity.

Question 11

Which of the following is a competitive inhibitor of an enzyme?

Accepted Answer

A molecule that binds to the active site, preventing substrate binding.

Question 12

Given the Michaelis-Menten equation $v = \frac{V_{max}[S]}{K_m + [S]}$, what happens to $V_{max}$ and $K_m$ in the presence of a non-competitive inhibitor?

Accepted Answer

$V_{max}$ decreases, $K_m$ remains unchanged.

Question 13

Which scenario best illustrates enzyme cooperativity?

Accepted Answer

Binding of one substrate molecule increases the enzyme's affinity for additional substrate molecules.

Question 14

A researcher plots $1/v$ versus $1/[S]$ for an enzyme-catalyzed reaction and obtains a straight line. What type of plot is this, and what does the y-intercept represent?

Accepted Answer

Lineweaver-Burk plot; y-intercept is $1/V_{max}$.

Question 15

Which of the following environmental factors can regulate enzyme activity in a cell?

Accepted Answer

Temperature, pH, cofactors, and inhibitors.

Question 16

Which of the following is true about the transition state of a chemical reaction?

Accepted Answer

It has the highest energy compared to reactants and products.

Question 17

If an enzyme-catalyzed reaction is performed at a pH far from the enzyme's optimum, what is the most likely effect?

Accepted Answer

The enzyme's activity will decrease due to altered active site structure.

Question 18

Which of the following best describes an allosteric inhibitor?

Accepted Answer

It binds to a site other than the active site, causing a conformational change that reduces enzyme activity.

Question 19

A metabolic pathway is regulated by feedback inhibition. Which statement best describes this process?

Accepted Answer

The final product of the pathway inhibits an enzyme involved early in the pathway.

Chapter 6: Bioenergetics, Enzyme Function, and Regulation

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