Cell Biology Exam 1

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Last updated 6:56 PM on 9/11/25
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112 Terms

1
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What are cells made of?

Macromolecules

2
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What drives what the cell can do?

Macromolecules

3
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What are the four basic combinations of atoms?

Macromolecules

4
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What are the small organic building blocks of the cell?

Sugars, fatty acids, amino acids, nucleotides

5
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What are the four macromolecules?

Carbohydrates, lipids, proteins, nucleic acids

6
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What are the structures of nucleotides?

Nitrogenous base, sugar, and phosphate group

7
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Does DNA or RNA use thymine?

DNA

8
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Does DNA or RNA use uracil?

RNA

9
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Does adenine or guanine have three bonds?

Guanine

10
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What is the basic structure of amino acids?

Amino group, carbon, carboxyl group

11
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Why do proteins have so many different functions?

They have so many different structures

12
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What do you look for to recognize a peptide bond?

C = O

13
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What are the levels of folding to create functional proteins?

Disulfide bonds, hydrogen bonds, ionic bonds, and Van der Waals and hydrophobic interactions

14
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What are lipids made up of?

Hydrophilic head and couple of hydrophobic fatty acid tails

15
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What is the hydrophilic head of a lipid made up of?

Polar group, phosphate, glycerol

16
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What causes variability in the lipid/phospholipid billayer?

Variability in the polar head group

17
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What is energy?

The capacity to cause specific physical or chemical changes

18
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Where do phototrophs get their energy from?

Light

19
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What are the different kinds of biological work?

Synthetic, mechanical, concentration, electrical, heat production, bioluminescence

20
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What is an example of synthetic work?

Photosynthesis

21
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What is an example of mechanical work?

The contraction of a weight lifter’s muscles

22
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What is an example of concentration work?

The accumulation of molecules in a cell

23
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What is an example of electrical work?

The membrane potential of a plant cell

24
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What is an example of heat production?

Shivering in the cold

25
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What is an example of bioluminescence?

The courtship of fireflies

26
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What is synthetic work?

Work of making something

27
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What is mechanical work?

Physical movement of something

28
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What is concentration work?

Accumulation of things

29
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What is electrical work?

Focus on charge aspect of an ion

30
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What is lost in the flow of energy?

Heat losses

31
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How does energy flow?

One way; it doesn’t cycle

32
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What membranes will be relatively stiff?

Contain mostly phospolipids with no double bonds

33
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What does the amphipathic nature of fatty acid-containing phospholipids do?

Drives the formation of a bilayer which serves to isolate water and hydrophilic molecules on either side

34
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What are the functions of carbohydrates?

Energy storage, structural stability, binding sites for proteins

35
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What does a positive change in entropy favor?

The progress of a reaction from reactants to products

36
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What process involves an increase in entropy of the system?

Combustion of paper

37
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What is the storage of glucose molecules by linking them together in the form of glycogen an example of?

Synthetic work

38
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What is entropy?

The measure of disorder or inability to do work in a system

39
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What is enthalpy?

The measure of total heat content in a system

40
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What is activation energy?

The minimum amount of energy reactants must contain before collisions between them will be successful in giving rise to products

41
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What does a catalyst do?

Lowers energy required for activation

42
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What is the active site?

The location on an ezyme where substrates bind and the catalysis occurs

43
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What is a reversible inhibitor?

Inhibitors that binds in a noncovalent matter, has free and bound forms

44
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What is an irreversible inhibitor?

Inhibitor that binds covalently to the enzyme and is usually toxic to cell

45
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What is substrate-level regulation?

Controlling the concentration of substrate available to the enzyme

46
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What is allosteric regulation?

Molecule other than substrate or immediate product regulates the enzyme

47
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What is covalent modification?

Addition or removal of a functional group/amino acid sequence to an enzyme that affects its conformation and ability to bind substrate

48
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What does covalent modification of phosphate groups do?

Regulates enzyme activity

49
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What do kinases do?

Add phosphate groups

50
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What do phosphotases do?

Dephosphorolate

51
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What are proenzymes?

Enzyme precursors, can become functional enzymes

52
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When is a chemical reaction spontaneous?

When the standard free energy change is negative

53
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When is a chemical reaction not spontaneous?

When the standard free energy change is positive

54
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What kind of work is a sodium/potassium pump an example of?

Concentration work

55
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What happens when Delta G = 0 in a chemical reaction?

Reactants and products are at equilibrium, no work can be done, no energy is required

56
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Why is the steady state vital to life possible?

The cell continually takes up energy from the environment

57
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What is the difference between how matter and energy flow through the biosphere?

Matter flows in cycles, whereas energy flows in one direction

58
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When cells maintain themselves in a steady state, which is vital to life, where are most of their reactions?

Far from thermodynamic equilibrium

59
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What does it mean to make a polymer?

Taking individual building blocks and sticking them together like legos

60
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What is special about polymers?

Like legos, they can be taken off and added to other places

61
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What is hydrophobicity?

The way molecules behave or react to water

62
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How does hydrophobicity affect molecules?

It gives molecular machines options for building

63
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What do molecules that do not interact well with water tend to do?

Cluster together and exclude both water and molecules that DO interact well with water

64
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What is a group with three phosphate groups called?

Triphosphate

65
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What does a prime (1’, 2’) symbol signal to look at?

The sugar instead of the nitrogenous base

66
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What is a phosphodiester?

A link between nucleotides, usually connected to a phosphate group

67
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What are the two chains of DNA brought together by?

Hydrogen bonding between nitrogenous bases

68
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How are DNA strands arranged?

Antiparallel to each other

69
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What do Purines always bond with?

Pyrimidine

70
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What is the backbone structure of all amino acids?

Amino group - carbon - carboxyl group

71
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Where does variation in amino acids come from?

Changes in the R group

72
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Which macromolecules have the most diversity in structures and therefore functions?

Proteins

73
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What is the strongest kind of bond, according to biology?

Covalent

74
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What is usually the strongest bond?

Ionic

75
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What tweaks the structure of a protein?

Hydrogen bonds breaking and forming

76
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What is the point to hydrogen bonds tweaking the structure of proteins?

Enables it to bind to something or let go of something

77
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What is the primary structure of proteins?

Sequence of amino acids

78
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What is the secondary structure of proteins?

Folded basic predictable structures of the amino acid sequence

79
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What is the tertiary structure of proteins?

Secondary structures that have been more folded into itself

80
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What do fatty acid tails heavily rely on to exclude water from the interior of the membrane?

Hydrophobicity

81
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What determines fluidity in the phospholipid bilayer?

The structure of fatty acids

82
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What is the variability in lipids caused by?

Variability in the polar head group

83
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What characteristic in the fatty acid tail causes the membrane to be more fluid?

More double bonds or kinks

84
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What are the pieces of polysaccharides called?

Monosaccharides

85
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What does it mean if the Delta H (change in heat) is positive?

The reaction is endothermic, it takes in heat

86
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What does it mean if the Delta H (change in heat) is negative?

The reaction is exothermic, it releases heat to its surroundings

87
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How are cells harnessing energy from one reaction to power another?

By constantly coupling reactions together

88
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When a reaction is exergonic, what is the released energy used for?

To make ATP

89
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What is a substrate?

The reactant or material being converted in a reaction

90
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What do the enzyme oxidoreductases do?

Catalyzes oxidation-reduction reactions, moves/removes whole hydrogen

91
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What do the enzyme transferases do?

Moves functional group from one molecule to another

92
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What do the enzyme hydrolases do?

Use water to break bonds

93
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What do the enzyme lyases do?

Remove or add a group from/to molecules, but isn’t necessarily a transfer

94
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What do the enzyme isomerases do?

Rearrange bonds within a molecule

95
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What do the enzyme ligases do?

Join two molecules together

96
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How does temperature affect the kinetic energy of molecules?

It affects how well the protein can fold into different conformations

97
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Which substrate binding model is more strongly supported by evidence?

Induced-fit model

98
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What is the lock-and-key model of substrate binding?

The shape of the substrate and the conformation of the active site are complementary to each other

99
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What is the induced-fit model for substrate binding?

The enzyme undergoes a change when binding to the substrate, BECOMING complementary after binding

100
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How does a competitive inhibitor work?

It binds to the active site, blocking the substrate and making no product

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