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Exergonic; spontaneous
Exergonic; endergonic
Free energy; entropy
Work; energy
Entropy; enthalpy
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Slightly increasing
Greatly increasing
Slightly decreasing
Greatly decreasing
No net change
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Increase the activation energy needed.
Cool the reactants.
Decrease the concentration of the reactants.
Add a catalyst.
Increase the entropy of the reactants.
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The universe loses energy because of heat production.
Systems rich in energy are intrinsically unstable and will give up energy with time.
Energy can be neither created nor destroyed.
The universe loses energy because of heat production and systems rich in energy are intrinsically unstable and will give up energy with time.
The universe loses energy because of heat production and systems rich in energy are intrinsically unstable, will give up energy with time, and energy can be neither created nor destroyed.
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Enzymes decrease the free energy change of a reaction.
Enzymes increase the rate of a reaction.
Enzymes change the direction of chemical reactions.
Enzymes are permanently altered by the reactions they catalyze.
Enzymes prevent changes in substrate concentrations.
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They do not depend on enzymes.
They consume energy to build up polymers from monomers.
They release energy as they degrade polymers to monomers.
They lead to the synthesis of catabolic compounds.
They do not depend on enzymes and they consume energy to build up polymers from monomers.
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Accessory enzyme
Allosteric group
Coenzyme
Functional group
Enzyme activator
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Potentiation
Cellular respiration
Digestion
Anabolism
Redox
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Catalysis
Metabolism
Anabolism
Dehydration
Catabolism
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Synthesis of macromolecules
Breakdown of macromolecules
Control of enzyme activity
Synthesis of macromolecules and breakdown of macromolecules
Synthesis of macromolecules, breakdown of macromolecules, and control of enzyme activity
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Entropy.
Activation energy.
Endothermic level.
Heat content.
Free-energy content.
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They are able to maintain a cooler internal temperature.
High temperatures make catalysis unnecessary.
Their enzymes have high optimal temperatures.
Their enzymes are insensitive to temperature.
They use molecules other than proteins as their main catalysts.
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Supplying the energy to speed up a reaction.
Lowering the energy of activation of a reaction.
Lowering the ΔG of a reaction.
Changing the equilibrium of a spontaneous reaction.
Increasing the amount of free energy of a reaction.
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Anabolism
Hydrolysis
Dehydration decomposition
Entropic
Dehydration synthesis
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Endergonic
Exergonic
Anabolic
Allosteric
Nonspontaneous
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Feedback regulation
Bioenergetics
Energy coupling
Entropy
Cooperativity
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Add more of the enzyme.
Heat the solution to 90°C.
Add more substrate.
Add an allosteric inhibitor.
Add a noncompetitive inhibitor.
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Endergonic.
Endothermic.
Enthalpic.
Spontaneous.
Exothermic.
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Enzymes may require a nonprotein cofactor or ion for catalysis to take place.
Enzyme function is reduced if the three-dimensional structure or conformation of an enzyme is altered.
Enzyme function is influenced by physical and chemical environmental factors such as pH and temperature.
Enzymes increase the rate of chemical reaction by lowering activation energy barriers.
All of the above are true of enzymes.
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EA
Products
Active sites
Reactors
Substrates
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Free energy of the system.
Free energy of the universe.
Entropy of the system.
Entropy of the universe.
Enthalpy of the universe.
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Metabolic inhibition.
Feedback inhibition.
Allosteric inhibition.
Noncooperative inhibition.
Reversible inhibition.
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By binding at the active site of the enzyme
By changing the structure of the enzyme
By changing the free energy change of the reaction
By acting as a coenzyme for the reaction
By decreasing the activation energy of the reaction
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Releasing heat upon hydrolysis.
Acting as a catalyst.
Coupling free energy released by ATP hydrolysis to free energy needed by other reactions.
Breaking a high-energy bond.
Binding directly to the substrate(s) of the enzyme.
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Enzymes are proteins that function as catalysts.
Enzymes display specificity for certain molecules with which they interact.
Enzymes provide activation energy for the reactions they catalyze.
The activity of enzymes can be regulated by other molecules.
An enzyme may be used many times over for a specific reaction.
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The energy content of an organism is constant.
The organism ultimately must obtain all of the necessary energy for life from its environment.
The entropy of an organism decreases with time as the organism grows in complexity.
Organisms are unable to transform energy.
Life does not obey the first law of thermodynamics.
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The products have more total energy than the reactants.
The reaction proceeds with a net release of free energy.
Some reactants will be converted to products.
A net input of energy from the surroundings is required for the reactions to proceed.
The reactions are nonspontaneous.
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Additional product would be formed.
Additional substrate would be formed.
The reaction would change from endergonic to exergonic.
The free energy of the system would change.
Nothing; the reaction would stay at equilibrium.
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It is not possible to determine whether an enzyme requires a cofactor from these data.
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Enzyme catalysis is dependent on the pH and temperature of the reaction environment.
Enzyme catalysis is dependent on the three-dimensional structure or conformation of the enzyme.
Enzymes provide activation energy for the reaction they catalyze.
Enzymes are composed primarily of protein, but they may bind nonprotein cofactors.
Enzyme activity can be inhibited if the enzyme's allosteric site is bound with a noncompetitive inhibitor.
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Negative ΔG, spontaneous
Positive ΔG, nonspontaneous
Positive ΔG, exergonic
Negative ΔG, endergonic
ΔG of zero, chemical equilibrium
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Denaturization of the enzyme
Allosteric inhibition
Competitive inhibition
Saturation of the enzyme activity
Insufficient cofactors
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ATP serves as a main energy shuttle inside cells.
ATP drives endergonic reactions in the cell by the enzymatic transfer of the phosphate group to specific reactants.
The regeneration of ATP from ADP and phosphate is an endergonic reaction.
ATP serves as a main energy shuttle inside cells and ATP drives endergonic reactions in the cell by the enzymatic transfer of the phosphate group to specific reactants.
ATP serves as a main energy shuttle inside cells, ATP drives endergonic reactions in the cell by the enzymatic transfer of the phosphate group to specific reactants, and regeneration of ATP from ADP and phosphate is an endergonic reaction.
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Competitive inhibitor of the enzyme.
Noncompetitive inhibitor of the enzyme.
Allosteric activator of the enzyme.
Cofactor necessary for enzyme activity.
Coenzyme derived from a vitamin.
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They combine molecules into more energy-rich molecules.
They are usually coupled with anabolic pathways to which they supply energy in the form of ATP.
They are endergonic.
They are spontaneous and do not need enzyme catalysis.
They build up complex molecules such as protein from simpler compounds.
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If the entropy of a system increases, there must be a corresponding decrease in the entropy of the universe.
If there is an increase in the energy of a system, there must be a corresponding decrease in the energy of the rest of the universe.
Every energy transfer requires activation energy from the environment.
Every chemical reaction must increase the total entropy of the universe.
Energy can be transferred or transformed, but it cannot be created or destroyed.
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Living organisms can convert energy among several different forms.
Living organisms can use energy to do work.
Organisms expend energy in order to decrease their entropy.
Living organisms can convert energy among several different forms and can use energy to do work.
Living organisms can convert energy among several different forms, can use energy to do work and expend energy in order to decrease their entropy.
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It is acquired by a reactant in an endergonic reaction.
It is used to convert an ATP into an AQP.
It is acquired by a reactant in a spontaneous reaction.
It is acquired by a reactant in an exergonic reaction.
It is broken down into one phosphorus and four oxygen atoms.
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A coenzyme.
An allosteric inhibitor.
The substrate.
An intermediate.
A competitive inhibitor.
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Conversion of energy from one form to another is always accompanied by some loss of free energy.
Heat represents a form of energy that cannot be used by most organisms to do work.
Without an input of energy, organisms would tend towards increasing entropy.
Cells require a constant input of energy to maintain their high level of organization.
Every energy transformation by a cell decreases the entropy of the universe.
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The starch solution has less free energy than the sugar solution.
The hydrolysis of starch to sugar is endergonic.
The activation energy barrier for this reaction cannot be surmounted.
Starch cannot be hydrolyzed in the presence of so much water.
Starch hydrolysis is nonspontaneous.
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A coenzyme
An allosteric inhibitor
A substrate
An intermediate
The product
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