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Cell Biology > Chapter 2 > Flashcards

Chapter 2 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What is the monomer for polysaccharides?

A

Sugars

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2
Q

What is the monomer for nucleic acids?

A

Nucleotides

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3
Q

What is the monomer for proteins?

A

Amino Acids

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4
Q

What is the monomer for lipids?

A

Fatty acids

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5
Q

What are Cis fats?

A

Type of double bond found in nature and leads to bending

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6
Q

What are trans fats?

A

Straighter fatty acids that are solid at room temperature

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7
Q

What is hydrogenation?

A

A process that results in double bonds in the trans orientation

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8
Q

What is a saturated fat?

A

Fatty acids with only single bonds

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9
Q

What is an unsaturated fat?

A

Fatty acids with double bonds

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10
Q

What do cholesterol and steroids function as?

A

Signaling molecules

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11
Q

How can cholesterol and steroids move through membranes?

A

Because they have no charge

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12
Q

What does cholesterol do?

A

Functions as a buffer for membranes

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13
Q

What is an amphipathic and what is an example?

A

Molecules that have both charged and uncharged portions.

Ex: detergents

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14
Q

What is a micelle?

A

Simplest structure in which water surrounds a single layer of phospholipids

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15
Q

What is a liposome and how do they assemble?

A

Bilayer structure used for delivery of small molecules or drugs assembled based on hydrophobic forces

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16
Q

What 3 components make up a Nucleic Acid?

A

Phosphate group, sugar, and nitrogenous base

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17
Q

What is a nucleic acid without the phosphate group called?

A

Nucleoside

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18
Q

Cytosine, thymine, uracil

A

Prymides

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19
Q

Adenine, guanine

A

Purines

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20
Q

What is the difference between prymides and purines?

A

Prymides are single ringed while purines have two rings

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21
Q

NAD+

A

Electron carrier for Kreb’s cycle

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22
Q

FAD

A

Secondary electron carrier

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23
Q

What are the components of an amino acid?

A

Amino group, carboxyl group, and a side chain

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24
Q

What is a polypeptide?

A

Long chain of amino acids

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25
Q

Describe polar charged.

A

1) Can form ionic bonds
2) Hydrophillic side chain can act as acids or bases
3) Active sites of enzymes

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26
Q

Which amino acids are in the polar charged group?

A 
Aspartic Acid
Glutamic Acid
Lysine
Arginine 
Histidine
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27
Q

Describe polar uncharged.

A

1) Form H- bonds
2) Associate with water
3) Hydrophillic side chains tend to have a partial (-) or (+) charge which allows for chemical reactions

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28
Q

Which amino acids are polar uncharged?

A 
Serine
Threonine 
Glutamine
Asparagine 
Tryosine
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29
Q

Describe non polar.

A

1) Hydrophobic side chain consists of C and H’s
2) Act as the inner core of soluble proteins
3) Associate with the lipid bilayer

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30
Q

Which amino acids are non polar?

A 
Alanine
Valine
Leucine 
Isoleucine 
Methionine
Phenylalanine
Tryptophan
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31
Q

Which amino acids are the only proteins that phosphate groups can bind to?

A

Serine, Threonine, and Tryosine

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32
Q

Which amino acids have side chains with unique properties?

A

Glycine
Cysteine
Proline

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33
Q

Alanine

A

Ala, A

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34
Q

Valine

A

Val, V

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35
Q

Aspartic Acid

A

Asp, D

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36
Q

Glutamic Acid

A

Glu, E

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37
Q

Lysine

A

Lys, K

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38
Q

Arginine

A

Arg, R

39
Q

Histidine

A

His, H

40
Q

Leucine

A

Leu, L

41
Q

Isoleucine

A

lIe, I

42
Q

Methionine

A

Met, M

43
Q

Phenylalanine

A

Phe, F

44
Q

Tryptophan

A

Try, W

45
Q

Serine

A

Ser, S

46
Q

Threonine

A

Thr, T

47
Q

Glutamine

A

Gln, Q

48
Q

Asparagine

A

Asn, N

49
Q

Tryosine

A

Try, Y

50
Q

Glycine

A

Gly, G

51
Q

Cysteine

A

Cys, C

52
Q

Proline

A

Pro, P

53
Q

What is a protein?

A

Large macromolecules that can contain 1 or more polypeptide chain

54
Q

Who developed the primary structure for amino acids?

A

Frederick Sanger

55
Q

Who was one of the only people who has won 2 individual noble prizes and developed the secondary structure for proteins?

A

Linus Pauling

56
Q

What is the tertiary structure of proteins?

A

The organization of alpha helices and beta sheets into complex structures

57
Q

What is the primary structure of proteins?

A

The sequencing of amino acids

58
Q

What is the secondary structure of amino acids?

A

Alpha Helices, Beta sheets, and a combination of both

59
Q

Give an example of a protein that only contains alpha helices

A

Myoglobin

60
Q

Give an example of a protein that only contains beta sheets

A

Green fluorescent protein

61
Q

Give an example of a protein containing both beta sheets and alpha helices

A

RAS

62
Q

What is the quaternary structure of proteins?

A

Made up of multiple polypeptide chains

63
Q

What are molecular machines and give an example.

A

Multi-protein interactions

Ex: ATP Synthase

64
Q

What hold protein domains together?

A

Intermolecular forces

65
Q

What are the characteristics of protein domains?

A

1) Proteins are modular
2) Proteins independently fold
3) Domains are associated with a function

66
Q

What is an interactome?

A

The entire collection of all interactions in the cell

67
Q

How are interactions within the cell described?

A

By a network map

68
Q

What are hub genes and why are they important?

A

In a network map, they are the genes that most of the arrows point to. They are important because a lot of theses genes are crucial to essential functioning within the cell

69
Q

What is a proteome?

A

The entire inventory of all proteins in the cell

70
Q

What are proteomics?

A

The study of all proteins in a cell by high computer assisted techniques

71
Q

What are thermodynamics?

A

The study of changes in energy in relation to events in the universe

72
Q

What are bioenergetics?

A

Specific to the transformation of energy within the cell

73
Q

What is the 1st Law of Thermodynamics?

A

Energy is conserved, energy cannot be created or destroyed

74
Q

What is the 2nd Law of Thermodynamics?

A

The tendency towards disorder (entropy)

75
Q

How is energy conserved at a cellular level?

A

Through catalysts

76
Q

What are catalysts?

A

Substances that stress chemical bonds and accelerates reactions in the forward or reverse reactions

77
Q

What are the biological catalysts?

A

Enzymes

78
Q

What did the Romans do and when?

A

In the first century, they used glass lenses as magnifiers

79
Q

What did Hans and Zaccharias do and when?

A

In the 1590s, they built the first microscope

80
Q

What did Anton Van Leeuwenhoek do and when?

A

In the mid 1600s, he improved lens grinding and increased magnification from 50 x to 270x

81
Q

What is the interacome?

A

The entire collection of all interactions in the cell.

82
Q

Name the three ways enzymes work.

A

1) Aligning the reactants to decrease activation entropy
2) Changing the reactivity of the substrate
3) Stress or alter the conformation of the substrate

83
Q

Why does thermodynamics matter in life?

A

Because cells are highly organized, therefore a lot of energy is needed to keep the organization

84
Q

Who came up with the graph used to measure enzyme activity?

A

Leonor Michaelis and Maud Menten

85
Q

How do reactions want to proceed?

A

To the lowest state of energy (entropy)

86
Q

Enzymes remain_________________after reactions.

A

The same

87
Q

What do enzymes sometimes require?

A

Cofactors such as metals to act as proton donors

88
Q

What are irreversible inhibitors?

A

Work by binding to an enzyme and reducing or eliminating its ability to catalyze a reaction

89
Q

What are Competitive Inhibitors?

A

They depend on the substrate and inhibitor to determine the velocity

90
Q

What are noncompetitive inhibitors?

A

Concentration of inhibitors determine reaction

91
Q

What is anabolism?

A

The synthesis of macromolecules

92
Q

What is catabolism?

A

The disassembly of macromolecules. ——>

93
Q

What does a negative delta G mean?

A

The reaction will occur spontaneously

94
Q

What does a positive delta G mean?

A

The reaction needs energy to occur

Cell Biology (4 decks)

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