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Biology > Chapter 8 Test > Flashcards

Chapter 8 Test Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Metabolism

A

The totality of an organism’s chemical reactions

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2
Q

Metabolic Pathway

A

Begins with specific molecule, which is then altered, resulting in a certain product

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3
Q

Catabolic pathway

A

Breakdown pathway

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4
Q

Anabolic pathway

A

Consumed energy to build complicated molecules from simpler ones

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5
Q

Energy

A

Capacity to cause change

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6
Q

Kinetic energy

A

Energy associated with relative motion of objects

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7
Q

Thermal energy

A

Kinetic energy associated with the random movement of atoms or molecules

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8
Q

Heat

A

Thermal energy in transfer from one object to another

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9
Q

Potential energy

A

Energy that is not kinetic; energy that matter processes because of its location or structure

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10
Q

Chemical energy

A

Potential energy available for release in a chemical reaction

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11
Q

1st law of thermodynamics

A

Energy of the universe is constant. Energy can be transferred and transformed, but it cannot be created or destroyed

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12
Q

Entropy

A

Measure of disorder, or randomness

The more randomly arranged a collection of matter is, the greater its entropy

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13
Q

2nd law of thermodynamics

A

Every energy transfer or transformation increases the entropy of the universe

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14
Q

Free energy

A

Portion of a system’s energy that can perform work when temperature and pressure are uniform throughout the system
🔺G = 🔺H - T🔺S

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15
Q

Exergonic reaction

A

Proceeds with a net release of free energy

  • 🔺G is negative
  • occurs spontaneously
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16
Q

Endergonic reaction

A

Absorbs free energy from its surroundings

  • 🔺G is positive (stores free energy)
  • non spontaneous
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17
Q

Enzyme

A

Macromolecule that acts as a catalyst

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18
Q

Catalyst

A

Chemical agent that speeds up a reaction without being consumed by the reaction

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19
Q

Activation energy

Free energy of activation

A

The initial investment of energy required to contort the reactant molecules so the bonds can break

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20
Q

Substrate

A

The reactant an enzyme acts on

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21
Q

Active site

A

A restricted region of the enzyme molecule that actually binds to the substrate

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22
Q

Induced fit

A

Binding between the enzyme and substrate become tighter after initial contact
-brings chemical groups of the active site into positions that enhance their ability to catalyze the chemical reaction

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23
Q

Cofactor

A

Nonprotein helpers for catalytic activity

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24
Q

Coenzyme

A

An organic molecule cofactor

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25
Q

Competitive inhibitor

A

Mimics that reduce the productivity of enzymes by blocking substrates from entering active sites

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26
Q

Feedback inhibition

A

A metabolic pathway is halted by the inhibitory binding of its end product to an enzyme that acts early in the pathway

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27
Q

Cooperativity

A

Mechanism amplified the response of enzymes to substrates: one substrate molecule primed an enzyme to act on additional substrate molecules more readily

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28
Q

Catabolic are

Anabolic are

A

Downhill

Uphill

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29
Q

Energy released from __ can be stored and then used to drive the uphill reactions of __

A

Catabolic pathways

Anabolic pathways

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30
Q

System

A

Matter under study

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31
Q

Surroundings

A

Everything outside the system

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32
Q

Isolated system

A

Unable to exchange either energy or matter with its surroundings

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33
Q

Open system

A

Energy and matter can be transferred between system and its surroundings

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34
Q

Spontaneous process

A

If a given process, by itself, leads to an increase in entropy, that process can proceed without requiring an input of energy

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35
Q

Nonspontaneous process

A

Leaders to decrease in entropy: will happen only if energy is supplies

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36
Q

The free energy change of a reaction tells us

A

Whether or not the reaction occurs spontaneously

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37
Q

Living systems increase

A

The entropy of their surroundings

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38
Q

🔺H

A

Change in system’s enthalpy

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39
Q

🔺S

A

Change in system’s entropy

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40
Q

T

A

Absolute temp in Kelvin

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41
Q

🔺G

A

Represents difference between free energy of final state and free energy of initial state

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42
Q

Spontaneous processes decrease…

A

System’s free energy

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43
Q

Processes that have a positive or zero 🔺G are

A

Never spontaneous

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44
Q

Spontaneous process 🔺G

A

Negative

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45
Q

Equilibrium

A

State of maximum stability

-a system at equilibrium cannot spontaneously change, it can do no work

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46
Q

Spontaneous implies

A

That it is energetically favorable, not that it will occur rapidly

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47
Q

Free energy

A

Measure of a system’s instability

-its tendency to change to a more stable state

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48
Q

Breaking bonds does not __, it __

A

Release energy

Requires energy

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49
Q

Reversible process cannot be downhill in both directions

A

Must be opposites: uphill and downhill

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50
Q

3 kinds of work a cell does

A

Chemical
Transport
Mechanical

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51
Q

Energy coupling

A

Use of an exergonic process to drive an endergonic process

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52
Q

ATP is responsible for mediating most energy coupling in cells and acts as immediate source of

A

Energy that powers cellular work

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53
Q

ATP releases energy when

A

Loses a phosphate group (hydrolysis)

54
Q

Phosphorylation

A

Transfer of a phosphate group from ATP to some other molecule
-the recipient molecule with the phosphate group covalently bonded to it: phosphorylated intermediate

55
Q

ATP is a renewable resource that can be regenerated by

A

The addition of a phosphate to ADP

-the free energy required to phosphorylate ADP comes from exergonic breakdown reactions in the cell

56
Q

Activation energy

A

Amount of energy needed to push the reactants to the top of an energy barrier, or uphill, so that the downhill part of the reaction can begin

57
Q

Enzymes…

A

Speed up metabolic reactions by lowering energy barriers

58
Q

Enzyme-substrate complex

A

When the enzyme bunds to its substrate

59
Q

Noncompetitive inhibitors

A

Do not directly compete with the substrate to bunt to the enzyme at the active site
-binds to another part of the enzyme and causes enzyme molecule to change shape so that the active site becomes less effective

60
Q

Spontaneous processes occur

A

Without energy input; they can happen quickly or slowly-happens with energy already there, doesn’t need more energy

61
Q

Entropy (disorder)

A

May decrease in an organism, but the universe will increase

62
Q

2nd law

A

Every energy transfer or transformation increases the entropy (disorder) of the universe
-energy is often lost as heat

63
Q

🔺G-Free energy

A

Energy that can do work when temperature and pressure are uniform
-the change in free energy (🔺G) during a process is related to the change in enthalpy, or change in total energy (🔺H), change in entropy (🔺S) and temp in Kelvin (T)

64
Q

Only processes with a negative 🔺G are

A

Spontaneous

65
Q

During spontaneous

A

Free energy decreases and the stability of a system increases

66
Q

Decrease in entropy

A

Dehydration reactions/synthesis

67
Q

Most free energy per molecule

A

Starch

68
Q

What does not represent an energy transformation?

A

The coupling of ATP hydrolysis to the production of a proton gradient across a membrane by a proton pump

69
Q

Greater free energy

A

Methane

70
Q

If during a process the system becomes more ordered, then

A

🔺S is negative

71
Q

When one molecule is broken down into 6 component molecules, which if the following will always be true?

A

🔺S is positive

72
Q

Negative 🔺G

A

Spontaneous
There is less energy than when you started
Free energy decreases
Stability of a system increases

73
Q

Which of the following is an example of the cellular work accomplished with the free energy derived from the hydrolysis of ATP, involved in the production of electrochemical gradients?

A

Proton movement against a gradient of protons

74
Q

Which of the following statements correctly describes some aspect of ATP hydrolysis being used to drive the active transport of an ion into the cell against the ion’s concentration gradient?

A

This is an example of energy coupling

75
Q

Much of the suitability of ATP as an energy intermediary is related to the instability of the bonds between the phosphate groups. These bonds are unstable because

A

The negatively charged phosphate groups vigorously repel one another and the terminal phosphate group is more stable in water than it is in ATP

76
Q

The formation of glucose-6-phosphate from glucose is an endergonic reaction and is coupled to which of the following reactions or pathways?

A

The hydrolysis of ATP

77
Q

What do the sign and magnitude of the ΔG of a reaction tell us about the speed of the reaction?

A

Neither the sign nor the magnitude of ΔG have anything to do with the speed of a reaction.

78
Q

Under most conditions, the supply of energy by catabolic pathways is regulated by the demand for energy by anabolic pathways. Considering the role of ATP formation and hydrolysis in energy coupling of anabolic and catabolic pathways, which of the following statements is most likely to be true?

A

High levels of ADP act as an allosteric activator of catabolic pathways

79
Q

What is meant by induced fit?

A

The binding between the enzyme and the substrate become tighter after initial contact

80
Q

Explain how protein structure is involved in enzyme specificity

A

The specificity of an enzyme results from its shape, which is determined by its amino acid sequence

81
Q

Many factors affect the rate of enzyme action.

Explain

A

Initial concentration of substrate: the more substrate molecules that are available, the more frequently they access the active site of the enzyme molecules
pH - 6-8 is best/optimal
Temperature: increase of temperature can increase rate, but too high temps can denature the protein molecule

82
Q

Why can extremes of pH or very high temperatures affect enzyme activity?

A

Extreme temperatures denature proteins and kill cells

83
Q

Cofactor

A

Nonprotein helpers for catalytic activity

84
Q

Coenzyme

A

If the cofactor is an organic molecule

85
Q

Allosteric regulation

A

Describes any case in which a protein/s function at one site is affected by the binding of a regulatory molecule to a separate site

86
Q

Allosteric regulation vs. Noncompetitive inhibition

A

They are similar in that allosteric inhibition may inhibit enzyme activity like nonconmpetitive, but different because it may also stimulate enzyme activity

87
Q

Allosteric activator vs. Allosteric inhibitor

A

The binding of an activator to a regulatory site stabilizes the shape that has functional active sites, whereas the binding of an inhibitor stabilizes the inactive form of the enzyme

88
Q

Explain the role of catabolic and anabolic pathways

A

Energy released from downhill reactions of catabolic pathways can be stored and then used to drive the uphill reactions

89
Q

Describe the relationship between free energy and equilibrium

A

The tendency for a reaction to reach equilibrium is driven by the Gibbs free energy

90
Q

Describe 3 main kinds of cellular work

A

Chemical work: pushing endergonic reactions
Transport work: pumping of substances across membranes against the direction of spontaneous movement
Mechanical work: movement of and within the cell

91
Q

3 components of ATP

A

Contains 3 phosphate groups, adenine, and ribose

92
Q

Describe the relationship between enzyme structure and enzyme specificity

A

The specificity of an enzyme results from its shape, which results from its amino acid sequence. The specificity of an enzyme is attributed to a compatible fit between the shape of its active site and the shape of the substrate

93
Q

Cell does 3 main types of work

A 
Chemical
Transport
Mechanical
-cells manage energy resources by energy coupling 
-powers by the hydrolysis of ATP
94
Q

The energy from the __ of ATP hydrolysis can be used to drive __

A

Exergonic reaction
Endergonic reaction
-couples reactions are exergonic

95
Q

Enzyme’s substrate

A

The reactant that an enzyme acts on

96
Q

Enzymes have high

A

Specificity

97
Q

Induced fit of a substrate

A

Brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction

98
Q

Rate of reaction increases as

A

Substrate concentration increases

99
Q

Transcription factor

A

Factors whether or not you can transcript it

100
Q

Enzymes can be controlled at

A

Transcription and concentration levels, shape and structure of enzyme can change

  • where you change it matters
  • changing the active site is what matters
101
Q

In an enzymatic reaction, the substrate

A

Binds to the active site of the enzyme

102
Q

The active site can lower an Ea barrier by:

A

Orienting substrates correctly -locking magnets into place
Straining substrate bonds
Providing a favorable micro environment

103
Q

Enzyme’s activity can be affected by

A

General environmental factors
-temp. and pH
Chemicals that specifically influence the enzyme
-enzymes have optimal temps and pH in which it can function

104
Q

Cofactors are nonprotein enzyme helpers

A

May be inorganic or organic

105
Q

Coenzyme

A

Organic cofactor

106
Q

Enzymes are proteins encoded by genes

A

-changes in genes lead to changes in amino acid composition of an enzyme

107
Q

Allosteric regulation

A

May either inhibit or stimulate an enzyme’s activity

  • occurs when a regulatory molecule brings to a protein at one site and affects the protein’s function at another site
  • can be inhibitor or activator
108
Q

Most allosterically regulated enzymes are made from

A

Polypeptide subunits -> quaternary

109
Q

Each enzyme has

A

Active and inactive forms

110
Q

The binding of an activator stabilizes the active form of an enzyme

A

Inhibitor/inactive

111
Q

Feedback inhibition

A

End product of a metabolic pathway shuts down the pathway

-prevents a cell from wasting chemical resources by synthesizing more product than needed

112
Q

Active site may resemble

A

A groove/pocket in protein into which the substrate fits

113
Q

Activation energy is changed

A

By presence of an enzyme

114
Q

Energy coupling

A

Exergonic reactions drive endergonic reactions

115
Q

Enzyme inhibitors: the action of inhibitors may be

A

Reversible or irreversible

116
Q

If the entropy of a living organism is decreasing

A

Energy input into the organism must be occurring to drive the decrease in entropy

117
Q

ATP drives mechanical work inside a cell by

A

Binding to motor proteins

Hydrolysis

118
Q

The activity of an enzyme and how effectively it functions is

A

Affected by general environmental factors

-temp and pH

119
Q

ATP drives transport work by

A

Phosphorylating a transport protein

120
Q

Competitive inhibitors bind…

While noncompetitive inhibitors…

A

To the active site of an enzyme

Bind away from the active site on an enzyme

121
Q

Allosteric regulation

A

Process of stabilizing the structure of an enzyme in its active form by the binding of a molecule
-describes any case in which a protein’s function at one site is affected by the binding of a regulatory molecule to another site

122
Q

ATP allosterically inhibits enzyme’s in ATP producing pathways. Result is called

A

Feedback inhibition

123
Q

ATP is a renewable resource because

A

ATP can be regenerated by the addition of a phosphate group to ADP

124
Q

🔺S would be positive for

A

Catabolism

125
Q

Energy in an ATP molecule is released through

A

Hydrolysis of one of the phosphate groups

126
Q

Enzymes speed up the rate of the reaction without

A

Changing the 🔺G for the reaction

127
Q

ATP in cellular metabolism

A

Free energy released by ATP hydrolysis may be coupled to an endergonic process via the formation of a phosphorylated intermediate

128
Q

Cofactors and coenzymes are both

A

Nonprotein helpers, but most cofactors are metal ions, and coenzymes are organic molecules that are a specific type of cofactor

129
Q

Enzymes can lower the activation energy of reactions, but they

A

Cannot change the net energy output

130
Q

Hydrolysis of ATP drives cellular work by

A

Releasing free energy that can be coupled to other reactions

Biology (16 decks)

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