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AP Biology > Chapter 3: The Chemical Building Blocks of Life > Flashcards

Chapter 3: The Chemical Building Blocks of Life Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What are the four types of organic molecules?

A

carbohydrates, lipids, proteins, nucleic acids

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2
Q

How many atoms can carbon bond to? What kinds of bonds can it form?

A

4, single, double, triple, quadruple

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3
Q

How many valence electrons does carbon have?

A

4

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4
Q

What is the backbone of biological molecules?

A

carbon

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5
Q

Hydrocarbons

A

molecules consisting of ONLY carbon and hydrogen

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6
Q

Where are many hydrocarbons found?

A

in many of a cell’s organic molecules

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7
Q

Isomers

A

molecules with the same molecular formula but different structures and properties

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8
Q

What are the three types of isomers?

A
  • structural
  • geometric
  • enantiomers
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9
Q

Structural isomers

A
  • isomers with differences in actual structure of their carbon skeletons
  • ex) glucose and fructose
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10
Q

Geometric (stereoisomers) isomers

A

have same carbon skeleton, but differ in how the groups are attached to the skeleton

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11
Q

Enantiomers

A
  • mirror images of each other
  • important in pharmaceutical industry
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12
Q

What are functional groups and their purpose?

A
  • parts of molecule involved in chemical reactions
  • chemically reactive groups of atoms within an organic molecule
  • give organic molecules distinct chemical properties
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13
Q

What are the 6 functional groups important to life?

A
  • hydroxyl
  • carbonyl
  • carboxyl
  • amino
  • sulfhydryl
  • phosphate
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14
Q

Hydroxyl group

A

hydrogen atom bonded to oxygen atom; this is bonded to the carbon skeleton

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15
Q

Carbonyl group

A

carbon atom double bonded to oxygen atom

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16
Q

Carboxyl group

A

oxygen atom is double bonded to a carbon atom, which is also bonded to a hydroxyl group (COOH)

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17
Q

Amino group

A

nitrogen bonded to two hydrogen atoms and to the carbon skeleton

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18
Q

Sulfhydryl group

A

sulfur atom bonded to hydrogen atom

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19
Q

Phosphate group

A

phosphorus atom bonded to four oxygen atoms; one oxygen bonded to carbon skeleton

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20
Q

Ketones

A

carbonyl group is within carbon skeleton

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21
Q

Aldehydes

A

carbonyl group at the end of the carbon skeleton

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22
Q

What type of bonds are the subunits of macromolecules joined by?

A

covalent bonds

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23
Q

Dehydration Synthesis

A
  • one molecule of water (H2O) is removed as subunits are linked with a bond
  • water is produced
  • anabolic (build up)
  • requires input of energy
  • enzymes carry out the breaking of bonds
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24
Q

Hydrolysis

A
  • molecule can be broken down into subunits as water is added
  • water is needed
  • catabolic
  • energy released
  • enzymes needed
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25
Q

Monomers

A

simplest unit of macromolecules

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26
Q

Polymer

A

large molecule made of repeating monomers

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27
Q

What are carbohydrates?

A

“sugars” and “starches”

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28
Q

What elements are found in carbs?

A

C, H, O

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29
Q

Ratio of C:H:O in carbs

A

1:2:1

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30
Q

Function of carbs

A
  • short term energy storage
  • structure
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31
Q

Examples of carbohydrate isomers

A

glucose, fructose, galactose

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32
Q

What kind of isomers are glucose and fructose

A

structural isomers, double bonded O is attached to diff carbons

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33
Q

What kind of isomers are glucose and galactose

A

stereoisomers, diff orientation of -OH groups

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34
Q

What are the most famous monosaccharides?

A

hexose sugars

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35
Q

How are disaccharides formed

A

2 monosaccharides connected by a covalent bond

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36
Q

Glucose + Glucose

A

Maltose

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37
Q

Glucose + Fructose

A

Sucrose

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38
Q

Glucose + Galactose

A

Lactose

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39
Q

What are big polymers of sugar called?

A

Polysaccharides

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40
Q

Function of glucose polymers

A
  • energy storage
  • structural support
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41
Q

Amylose (starch)

A
  • used for energy storage in plants
  • alpha linked
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42
Q

Glycogen

A

used for energy storage in animals, stored in liver and muscles

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43
Q

Cellulose

A
  • major component of plant-like cell walls
  • beta linked
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44
Q

Pectin

A

branched chains with short linear amylose branches found in plants

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45
Q

Why is cellulose difficult to digets?

A

orientation of glucose subunits (CH2OH) are on opposite sides, so it is hard to break the bonds

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46
Q

Chitin

A
  • structural support in fungi cell walls
  • exoskeleton of insects
  • dissolving stiches
  • modified polysaccharide
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47
Q

How do herbivores digest cellulose?

A

cows have bacteria that can break down cellulose

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48
Q

Peptidoglycan

A
  • in bacterial cell walls
  • modified peptidoglycan
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49
Q

What are the 3 ways that carbohydrates are used in organisms?

A

1.) kept as glucose/immediate energy
2.) converted to transport disaccharides
3.) converted to starch, glycogen, or fat, and used in the future

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50
Q

What are common lipids?

A

fats, oils, waxes

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51
Q

What elements are found in lipids?

A

C, H, O

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52
Q

Ratio of H:O in lipids

A

greater than a 2:1 ratio

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53
Q

Function of lipids

A
  • long term energy storage
  • insulation
54
Q

Unique characteristic of lipids

A

insoluble in water - expose hydrophilic (polar) parts in water, but protect their hydrophobic (nonpolar) parts

55
Q

What are the three major groups of lipids?

A
  • triglycerides
  • phospholipids
  • steroids
56
Q

What are triglycerides made of?

A

3 fatty acids and 1 glycerol

57
Q

What are triglycerides connected by?

A
  • dehydration synthesis
  • ester bonds
58
Q

Saturated triglyceride

A
  • no double bonds between carbons
  • saturated with hydrogen
59
Q

Unsaturated triglyceride

A
  • at least one double bond
  • often liquid at room temperature because the double bond creates a bend in the tail that prevents the tight packing of molecules
60
Q

What do phospholipids make up?

A

the cell membrane

61
Q

What makes up a phospholipid?

A

a glycerol, 2-fatty acids, and a phosphate group

62
Q

Phospholipid nickname

A

modified triglyceride

63
Q

What kind of molecule is a phospholipid?

A

amphipathic

64
Q

Glycerol

A

3 carbon alcohol molecule that forms backbone of phospholipids

65
Q

2 Fatty Acids in phospholipids

A

long hydrocarbon chains ending in a carboxyl group

66
Q

Where is the phosphate group of a phospholipid attached to?

A

attached to one end of the glycerol

67
Q

How are the layers of phospholipids forms?

A

tails point towards each other

68
Q

What is responsible for the ability of fats to store energy for long periods?

A

energy is stored in the C-H bonds, which are harder to break down because they are nonpolar

69
Q

More than one double/triple bond in a fat is considered…

A

polyunsaturated

70
Q

How many water molecules are lost in the synthesis of 1 fatty acid? How many bonds are formed?

A
  • 3 water molecules lost
  • 3 bonds formed
71
Q

Are plant fats usually liquid or solid at room temp?

A

liquid

72
Q

Are animal fats usually liquid or solid at room temp?

A

solid

73
Q

How can oil be converted into a solid?

A

Add hydrogen (hydrogenated)

74
Q

Terpenes

A
  • long chain lipids that make up many pigments (chlorophyll, retinal)
  • ex) rubber
75
Q

Steroids

A
  • 1 class of hormones and cholesterol
  • 4 carbon rings
76
Q

Where is cholesterol found?

A

in the cell membrane

77
Q

Examples of hormones

A
  • testosterone
  • estrogen
78
Q

What is responsible for the different functions of steroids?

A

different functional groups

79
Q

Prostaglandin

A
  • a group of 20 lipids that are modified fatty acids
  • help communicate between cells
  • aspirin holds back prostaglandin to reduce pain
80
Q

Are carbs or fats more efficient for energy storage and why?

A
  • fats because they contain over 40 carbon atoms
  • fats yield 9 kcal of energy/gram vs cabrs yeild 4 kcal of energy/gram
81
Q

Elements in proteins

A

C, H, O, N, sometimes S

82
Q

Why are proteins the most complex biological molecule?

A

because of all the possible amino acid sequences

83
Q

What determines a proteins function?

A

specific amino acid sequence

84
Q

What are proteins made of?

A

polymers of amino acids monomers

85
Q

What kind of bonds connect amino acids

A

peptide (covalent) bonds

86
Q

Globular proteins

A
  • ex) enzymes, antibodies, transport proteins
87
Q

Fibrous proteins

A
  • for structure and support
  • keratin, actin & myosin, collagen
88
Q

Peptides

A
  • hormones, intercellular messengers
89
Q

How many known amino acids are there?

A

21

90
Q

Structure of an amino acid

A
  • amino group (NH2) and carboxyl group (COOH) bonded to a central alpha carbon
  • R side chain varies and determines the solubility and identity of the amino acid
91
Q

Directionality in amino acids

A
  • N-terminus is the amino end
  • C-terminus is the carboxyl end
92
Q

What are the 5 classes of amino acids based on their R groups?

A
  • nonpolar
  • polar (uncharged)
  • ionizable
  • aromatic
  • special function
93
Q

Nonpolar amino acids

A

R groups have CH2 or CH3

94
Q

Polar (uncharged) amino acids

A

R groups have only H or OH

95
Q

Ionizable amino acids

A

R groups have acids/bases

96
Q

Aromatic amino acids

A

R groups have an organic ring with an alternating single/double bond

97
Q

Special function amino acids

A
  • specific properties
  • methionine = initiates protein synthesis
  • proline = caused kinks in chain
  • cysteine - links chains together
98
Q

Dipeptide

A

2 amino acids joined to make a molecule

99
Q

Polypeptide

A

chain of amino acid sequence

100
Q

What determines a protein’s function?

A

its shape

101
Q

What can be used to determine a protein’s shape?

A

x-ray diffraction

102
Q

What are the 4 levels of protein structure?

A

1.) Primary structure
2.) Secondary structure
3.) Tertiary structure
4.) Quaternary structure

103
Q

Primary structure of a protein

A
  • the sequence of amino acids in one polypeptide chain
  • peptide (covalent) bonds between amino acids
104
Q

Secondary structure of a protein

A
  • regular, repeating 3D structures found in all polypeptide chains
  • alpha helix
  • beta sheet
  • folds are called motifs
  • hydrogen bonding within the primary chain between the C double bonded to O and H of NH
105
Q

Tertiary structure of a protein

A
  • final folded shape of a specific polypeptide chain
  • bonds are between the R groups (hydrogen bonds, ionic bonds, disulfide bridges, hydrophobic interactions)
  • driven by hydrophobic interactions
106
Q

Domains

A

sections of the tertiary structure with different functions

107
Q

Quaternary structure of a protein

A
  • the specific 3D shape of a protein that is made of more than one polypeptide chain (each with own tertiary structure)
  • only “optional” level of structure
  • happens from the overall structure when multiple chains form a functional protein
  • bonds are between the R groups (hydrogen bonds, ionic bonds, disulfide bridges, hydrophobic interactions)
108
Q

What are the 8 different types of proteins?

A
  • storage
  • structural
  • transport
  • contractile/motor
  • hormonal
  • defensive
  • receptor
  • enzymatic
109
Q

What are proteins responsible for?

A

all life activities of the cell

110
Q

Sickle cell anemia

A
  • results from valine (hydrophobic) replacing glutamic acid (hydrophilic) in beta chains of hemoglobin
111
Q

What does hemoglobin do?

A

it carries oxygen in red blood cells

112
Q

Chaperone proteins

A

help new proteins fold correctly

113
Q

Denaturation

A
  • if a protein’s environment is altered
  • most of the time cannot be reversed
  • denaturation = change in structure of a protein; inactive
  • protein shape changes, but bonds do not
114
Q

What conditions can denature proteins?

A

pH, temperature, concentration

115
Q

Renaturation

A

the ability of a small protein to spontaneously refold into its original shape with the normal environment is established - shows relation of primary and tertiary structure

116
Q

Nucleic Acids function

A

information storage for biological systems

117
Q

What elements are nucleic acids made of?

A

C, H, O, N, P

118
Q

What are nucleic acids polymers of?

A

nucleotides

119
Q

What are polymers of nucleotides linked by?

A

phosphodiester bonds (btwn phosphate of one nucleotide and sugar of next nucleotide)

120
Q

Nucleotide structure

A
  • phosphate
  • pentose sugar
  • nitrogenous base
121
Q

DNA function

A
  • stores info about primary structure of proteins and sequences of RNA molecules
  • heritable
  • encodes info
122
Q

RNA function

A
  • reads info and directs protein synthesis
  • transmits and translates DNA info into protein
  • many enzymatic and regulatory functions
  • 15 known types of RNA
123
Q

What are the three types of RNA?

A
  • messenger
  • transfer
  • ribosomal
124
Q

DNA characteristics

A
  • deoxyribose sugar
  • bases: adenine, thymine, guanine, cytosine
  • double helix
  • 2 chains of covalently bonded nucleotides
  • chains are bonded to each other by hydrogen bonds between the nitrogenous bases
125
Q

RNA characteristics

A
  • ribose sugar
  • bases: adenine, uracil, guanine, cytosine
  • single strand
  • less stable than DNA
126
Q

Polynucleotides different ends

A
  • phosphate on one end (5’) and an OH from a sugar on the other end (3’)
  • numbers come from carbon numbering of the sugar
127
Q

Who discovered DNA structure?

A
  • Watson and Crick published the paper
  • Wilkins and Franklin did the X-ray diffraction
  • won the Nobel prize for it in 1962
128
Q

Purines

A
  • large double ring molecules
  • adenine and guanine
129
Q

Pyrimidines

A
  • smaller, single-ring molecules
  • cytosine, thymine, uracil
130
Q

What nucleotides are used as electron carriers?

A
  • nicotinamide adenine dinucleotide
  • flavin adenine dinucleotide
131
Q

How does information travel?

A
  • info stored in DNA goes to RNA before some of the info is used to direct the construction of proteins - “Central Dogma” of molecular biology
132
Q

What is ATP?

A
  • the energy currency of the cell
  • adenosine triphosphate
  • high energy molecule produced as a result of respiration
  • contains the nucleotide base adenine

AP Biology (5 decks)

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