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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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Catalysis
Metabolism
Anabolism
Dehydration
Catabolism
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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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They do not depend on enzymes.
They are highly regulated sequences of chemical reactions.
They consume energy to build up polymers from monomers.
They release energy as they degrade polymers to monomers.
They are highly regulated sequences of chemical reactions and they consume energy to build up polymers from monomers.
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Energy cannot be created or destroyed.
The entropy of the universe is decreasing.
The entropy of the universe is constant.
Kinetic energy is stored energy that results from the specific arrangement of matter.
Energy cannot be transferred or transformed.
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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 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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Living organisms do not obey the second law of thermodynamics, which states that entropy must increase with time.
Life obeys the second law of thermodynamics because the decrease in entropy as the organism grows is balanced by an increase in the entropy of the universe.
Living organisms do not follow the laws of thermodynamics.
As a consequence of growing, organisms create more disorder in their environment than the decrease in entropy associated with their growth.
Living organisms are able to transform energy into entropy.
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Metabolism is an emergent property of life at the level of organisms.
Metabolism manages the utilization of materials and energy resources.
The uptake of water associated with the hydrolysis of biological polymers is part of metabolism.
Metabolism depends on a constant supply of energy.
None of these statements about metabolism is incorrect.
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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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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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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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Light energy
Electrical energy
Thermal energy (heat)
Mechanical energy
Potential energy
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Dehydration reactions
Hydrolysis
Respiration
Digestion
Catabolism
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The synthesis of large molecules from small molecules is exergonic.
Earth is an open system.
Life exists at the expense of energy derived from its environment.
A living cell can never function as a closed system.
Every chemical reaction in a cell results in a loss of free energy.
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Is consistent with the second law of thermodynamics.
Requires that due to evolution, the entropy of the universe increased.
Is based on the fact that organisms function as closed systems.
Is consistent with the second law of thermodynamics and requires that due to evolution, the entropy of the universe increased.
Is consistent with the second law of thermodynamics, requires that due to evolution, the entropy of the universe increased, and is based on the fact that organisms function as closed systems.
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ΔS is the change in entropy, a measure of randomness.
ΔH is the change in enthalpy, the energy available to do work.
ΔG is the change in free energy.
T is the absolute temperature.
ΔS is the change in entropy, a measure of randomness, and ΔH is the change in enthalpy, the energy available to do work.
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Slightly increasing
Greatly increasing
Slightly decreasing
Greatly decreasing
No net change
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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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A reaction in which the free energy at equilibrium is higher than the energy content at any point away from equilibrium
A chemical reaction in which the entropy change in the reaction is just balanced by an opposite entropy change in the cell's surroundings
An endergonic reaction in an active metabolic pathway where the energy for that reaction is supplied only by heat from the environment
A chemical reaction in which both the reactants and products are only used in a metabolic pathway that is completely inactive
There is no possibility of having chemical equilibrium in any living cell.
+ΔH, +ΔS, +ΔG
+ΔH, -ΔS, -ΔG
+ΔH, -ΔS, +ΔG
-ΔH, -ΔS, +ΔG
-ΔH, +ΔS, +ΔG
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+ΔG, +ΔH, +ΔS
+ΔG, +ΔH, -ΔS
+ΔG, -ΔH, -ΔS
-ΔG, +ΔH, +ΔS
-ΔG, -ΔH, -ΔS
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Endergonic.
Endothermic.
Enthalpic.
Spontaneous.
Exothermic.
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Its hydrolysis provides an input of free energy for exergonic reactions.
It provides energy coupling between exergonic and endergonic reactions.
Its terminal phosphate group contains a strong covalent bond that when hydrolyzed releases free energy.
Its hydrolysis provides an input of free energy for exergonic reactions and it provides energy coupling between exergonic and endergonic reactions.
Its hydrolysis provides an input of free energy for exergonic reactions and it provides energy coupling between exergonic, endergonic reactions, and its terminal phosphate group contains a strong covalent bond that when hydrolyzed releases free energy. .
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Has a ΔG of about -7 kcal/mol under standard conditions.
Involves hydrolysis of a terminal phosphate bond of ATP.
Can occur spontaneously under appropriate conditions.
Has a ΔG of about -7 kcal/mol under standard conditions and involves hydrolysis of a terminal phosphate bond of ATP.
Has a ΔG of about -7 kcal/mol under standard conditions, involves hydrolysis of a terminal phosphate bond of ATP, and can occur spontaneously under appropriate conditions.
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Cells are open systems, but a test tube is a closed system.
Cells are less efficient at heat production than nonliving systems.
The hydrolysis of ATP in a cell produces different chemical products than does the reaction in a test tube.
The reaction in cells must be catalyzed by enzymes, but the reaction in a test tube does not need enzymes.
Cells convert some of the energy of ATP hydrolysis into other forms of energy besides heat.
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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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A + Pi → AP (ΔG = +10 kcal/mol)
B + Pi → BP (ΔG = +8 kcal/mol)
CP → C + Pi (ΔG = -4 kcal/mol)
DP → D + Pi (ΔG = -10 kcal/mol)
E + Pi → EP (ΔG = +5 kcal/mol)
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An anabolic steroid
A DNA helix
RNA nucleotides
An amino acid with three phosphate groups attached
A phospholipid
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Feedback regulation
Bioenergetics
Energy coupling
Entropy
Cooperativity
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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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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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The reaction is faster than the same reaction in the absence of the enzyme.
The free energy change of the reaction is the same as the reaction in the absence of the enzyme.
The reaction always goes in the direction toward chemical equilibrium.
The reaction is faster than the same reaction in the absence of the enzyme and the free energy change of the reaction is the same as the reaction in the absence of the enzyme.
The reaction always goes in the direction toward chemical equilibrium, the free energy change of the reaction is the same as the reaction in the absence of the enzyme, and the reaction always goes in the direction toward chemical equilibrium.
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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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Bringing glucose and fructose together to form sucrose.
The release of water from sucrose as the bond between glucose and fructose is broken.
Breaking the bond between glucose and fructose and forming new bonds from the atoms of water.
Production of water from the sugar as bonds are broken between the glucose monomers.
Utilization of water as a covalent bond is formed between glucose and fructose to form sucrase.
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Entropy.
Activation energy.
Endothermic level.
Heat content.
Free-energy content.
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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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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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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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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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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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-40 kcal/mol
-20 kcal/mol
0 kcal/mol
+20 kcal/mol
+40 kcal/mol
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Binds allosteric regulators of the enzyme.
Is involved in the catalytic reaction of the enzyme.
Binds the products of the catalytic reaction.
Is inhibited by the presence of a coenzyme or a cofactor.
Binds allosteric regulators of the enzyme and is involved in the catalytic reaction of the enzyme.
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The binding of the substrate depends on the shape of the active site.
Some enzymes change their structure when activators bind to the enzyme.
A competitive inhibitor can outcompete the substrate for the active site.
The binding of the substrate changes the shape of the enzyme's active site.
The active site creates a microenvironment ideal for the reaction.
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Changes in the activation energy of the reaction
Changes in the active site of the enzyme
Changes in the free energy of the reaction
Changes in the activation energy of the reaction and in the active site of the enzyme
Changes in the activation energy of the reaction, in the active site of the enzyme, and in the free energy of the reaction
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1
2
3
4
5
1
2
3
4
5
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1
2
4
5
It is not possible to determine whether an enzyme requires a cofactor from these data.
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Fewer substrates have sufficient energy to get over the activation energy barrier.
Motion in the active site of the enzyme is slowed, thus slowing the catalysis of the enzyme.
The motion of the substrate molecules decreases, allowing them to bind more easily to the active site.
Fewer substrates have sufficient energy to get over the activation energy barrier and motion in the active site of the enzyme is slowed, thus slowing the catalysis of the enzyme.
Fewer substrates have sufficient energy to get over the activation energy barrier, motion in the active site of the enzyme is slowed, thus slowing the catalysis of the enzyme, and the motion of the substrate molecules decreases, allowing them to bind more easily to the active site.
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