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Biological molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What are monomers?

A

Small units which are components of larger molecules

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2
Q

What are polymers?

A

Molecules made from monomers joined together

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3
Q

What is a condensation reaction?

A

Joins monomers together by chemical bonds. Eliminates a water molecule

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4
Q

What is a hydrolysis reaction?

A

Water is added to break a chemical bond between two molecules. (Opposite of condensation)

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5
Q

Chemical elements that make up carbohydrates

A

C,H,O

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6
Q

Chemical elements that make up lipids

A

C,H,O

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7
Q

Chemical elements that make up proteins

A

C,H,O,N,S

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8
Q

Chemical elements that make up nucleic acids

A

C,H,O,N,P

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9
Q

Which way is the OH group facing on carbon 1 in alpha glucose?

A

Downwards

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10
Q

Which way is the OH group facing on carbon 1 in beta glucose?

A

Upwards

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11
Q

Glucose properties

A

Water soluble (as the molecule is polar and forms hydrogen bonds)
Provides energy for ATP production

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12
Q

What is a monosaccharide?

A

A single sugar molecule

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13
Q

What is a disaccharide?

A

A molecule comprising of two monosaccharides joined by a glycosidic bond

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14
Q

What is a polysaccharide?

A

A polymer made of many sugar monomers

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15
Q

What is a hexose sugar?

A

Monosaccharide with 6 carbons

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16
Q

What is a pentose sugar?

A

A monosaccharide with 5 carbons

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17
Q

Ribose properties

A

Water soluble
Component of RNA nucleotides

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18
Q

Two monosaccharides that make up maltose

A

two alpha glucose molecules

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19
Q

Where is maltose found?

A

In germinating seeds

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20
Q

Where is glucose found?

A

Fruit

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21
Q

Two monosaccharides that make up sucrose

A

alpha? glucose and fructose

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22
Q

Where is sucrose found?

A

In phloem tissue and fruit

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23
Q

Where is fructose found?

A

Fruit and nectar

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24
Q

Two monosaccharides that make up lactose

A

alpha? glucose and galactose

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25
Q

Where is lactose found?

A

In milk/ milk products

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26
Q

Where is galactose found?

A

In milk

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27
Q

Which are the most and least sweet out of glucose, fructose and sucrose?

A

Fructose is the most sweet
Galactose is the least sweet

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28
Q

What is the bond formed between to alpha glucose molecules after a condensation reaction?

A

1,4 glycosidic bond (or 1,6)

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29
Q

What is starch?

A

Many alpha glucose molecules
Glucose is stored as starch.
Two forms

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30
Q

What are the two forms of starch?

A

Amylose
Amylopectin

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31
Q

Shape of amylose

A

Coils into helix (due to hydrogen bonding)

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32
Q

Amylose properties

A

Long chain
Unbranched
alpha glucose
1,4 glycosidic bonds
Compact
Less soluble
(Plants)

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33
Q

Amylopectin properties

A

Long chain
Branched
alpha glucose
1,4 and 1,6 glycosidic bonds
Insoluble
(Plants)

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34
Q

Glycogen properties

A

Chain
Branched - more than amylopectin
alpha glucose
1,4 and 1,6 glycosidic bonds
Compact
Insoluble
(Animals)

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35
Q

Why is the breakdown of glycogen faster than amylose?

A

It has more free ends where glucose molecules can be added or removed. Speeds up the storing/releasing of glucose molecules. Therefore suited to storage role.

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36
Q

Cellulose properties

A

straight - chain molecule
Unbranched
Beta glucose (each alternative one is rotated 180)
1,4 glycosidic bond
Strong
Insoluble (makes cell walls)

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37
Q

Formation of fibres from cellulose

A

Many chains are cross linked by hydrogen bonds to form microfibrils.
Many microfibrils are cross linked to form macrofibrils.
Combine to form cellulose fibres.

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38
Q

Why is cellulose important for a healthy digestive system?

A

It’s hard to break down. Forms fibre and roughage.

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39
Q

How do the properties of glucose relate to its function?

A

Polar - soluble in water (dissolve in cytosol of cell)
Small - can travel through the bloodstream and into/out of cells

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40
Q

How do the properties of amylose relate to its function?

A

Helix shape - compact so its energy dense a good storage molecule
Insoluble - doesn’t affect water potential

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41
Q

How do the properties of amylopectin relate to its function?

A

Branched - increase surface area for enzyme so can be hydrolysed quickly
Insoluble - good storage molecule

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42
Q

How do the properties of glycogen relate to its function?

A

More branched - compact and energy dense - used for storage
Hydrolysed quickly than starch - animals need glucose faster due to higher metabolic rate

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43
Q

How do the properties of cellulose relate to its function?

A

Mechanical strength - strong fibres due to hydrogen bonding
Insoluble - difficult to break down
Gaps between fibres - permeable cell walls

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44
Q

State of lipids at room temperature

A

Liquid = oils
Solid = fats

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45
Q

What is a triglyceride made up of?

A

Glycerol and 3 fatty acids

46
Q

What bond is there in a trigylceride?

A

Ester bond

47
Q

Why are lipids non-polar?

A

Outer electrons form evenly distributed bonds, so there are no +ve or -ve areas

48
Q

What is a macromolecule?

A

A large complex molecules with a larger molecular weight - containing a lot of atoms

49
Q

What types of reaction is esterification?

A

Condensation

50
Q

What is saturated?

A

No double bonds in the fatty acid chain

51
Q

What is monounsaturated?

A

One double bond

52
Q

What is polyunsaturated?

A

Two or more double bonds

53
Q

How saturation affects room temperature state?

A

A molecule with more double bonds cannot pack as closely together - as double bonds make the molecule bend. Therefore they are liquid at room temperature = oils

54
Q

Which is healthier, saturated or unsaturated?

A

Unsaturated (more double bonds = oils = healthier)

55
Q

What is a phospholipid?

A

Has a phosphate ion (PO43-) and only two fatty acids.

56
Q

Why is the head of a phospholipid hydrophobic?

A

Th phosphate ion has extra electrons which are negatively charged, so is hydrophobic (soluble in water).

57
Q

Why are the tails of a phospholipid hydrophilic?

A

They are non-polar

58
Q

How do phospholipids interact with water?

A

Form a layer on the surface of the water - they are therefore surfactants
Form cell membranes - bilayer which separates the outside aqueous environment from the cytosol inside the cell. (hydrophobic tails on inside and hydrophilic heads on outside)

59
Q

Where are ester bonds when a trugylcerde/phosphpolipid is formed?

A

Hydroxyl from COOH on the fatty acid and a H from the hydroxyl group on the glycerol

60
Q

Hydrolysis of triglycerides

A

3 molecules of water supplied and ester bonds are broken

61
Q

How do the properties of triglycerides relate to their function?

A

Long term energy storage
Thermal insulation
Cushioning - protect vital organs
Buoyancy for aquatic animals
Electrical insulation around nerves

62
Q

How do the properties of cholesterol relate to their function?

A

Have a hydrophilic OH group (the rest is hydrophobic).
Regulates fluidity of membranes
Hormone production

63
Q

What are sterols?

A

Complex alcohol molecules

64
Q

How do the properties of phospholipids relate to their function?

A

Membrane bilayers
Creating of hydrophobic barriers

65
Q

The general structure of the amino acid

A

Amine group = basic
R group = variable side chain
Carboxyl group = acidic

66
Q

How many different amino acids are there?

A

20

67
Q

What bonds are formed between amino acids?

A

Peptide (covalent)

68
Q

What is a dipeptide?

A

Two amino acids

69
Q

What is a polypeptide?

A

Three or more amino acids

70
Q

How is a peptide bond formed?

A

OH from carboxylic group and H from amine group

71
Q

What is the condensation reaction of amino acids catalysed by?

A

Peptidyl transferase

72
Q

How do proteins have specificity?

A

Different amino acid sequence = different bonds/interactions between r groups = folds into different structures with different shapes = specific

73
Q

What is the primary structure of proteins?

A

Sequence of amino acids

74
Q

Bonds in primary structure

A

peptide bonds

75
Q

What are the two secondary structures of proteins?

A

alpha helix
b pleated sheets

76
Q

What happens in secondary structure?

A

Negatively (weak) charged N an O interact with weakly positive H atoms

77
Q

Bonds in secondary structure

A

Peptide bonds
Hydrogen bonds

78
Q

What happens in tertiary structure?

A

Bonds form between R groups

79
Q

Bonds in tertiary structure

A

Peptide
Hydrogen (weakest but most common)
Disulphide bonds - covalent/ strongest
Ionic - Between oppositely charged r groups (stronger than H bonds but no common)
Hydrophobic/hydrophilic interaction - form between non-polar r groups within interior of protein

80
Q

What is quaternary structure?

A

2 or more subunits (polypeptides)
Interactions are the same as tertiary but are between protein molecules rather than with one.

81
Q

What is the hydrolysis of polypeptides catalysed by?

A

Proteases enzymes

82
Q

Structure of globular proteins

A

Roughly spherical (teritary)
Soluble (hydrophilic r groups on outside, hydrophobic on inside)
Compact
Have a very specific shape
Physiological. functional functions

83
Q

What is insulin?

A

A globular protein
Hormone secreted by the pancreas that regulates blood glucose concentration

84
Q

Structure of insulin

A

alpha helix and beta pleated sheet (two polypeptide chains) held by disulphide bridges

85
Q

Why insulin being a globular protein in useful for its function?

A

Hormones travel in blood so need to be soluble
Need to fit into specific receptors so need specific shapes

86
Q

What are conjugated proteins?

A

Globular proteins that contain a prosthetic group

87
Q

What is a prosthetic group?

A

A non-protein component

88
Q

What are proteins without a prosthetic group called?

A

Simple proteins

89
Q

Examples of prosthetic groups

A

Lipids - Lipoproteins
Carbohydrates - Glycoproteins
Metal ions
Molecules derived from vitamins

90
Q

What is a haem group?

A

Contain an iron ion (Fe2+).

91
Q

Structure of haemoglobin

A

Globular
Conjugated
Quaternary
4 polypeptides (2 alpha and 2 beta)
4 prosthetic haem groups
Iron ion combines with O2 molecules to allow it to carry oxygen around the body

92
Q

Structure of catalase

A

Enzyme
Quaternary
4 haem prosthetic groups

93
Q

How the structure of catalase relates to its function?

A

Iron ion allows it to interact with hydrogen peroxide (H2O2) and speed up its breakdown.
H2O2 is a common by-product of metabolism but is damaging to cell/cell components
Catalase ensures it doesn’t accumulate - converts H2O2 into H2O and O2

94
Q

Structure of fibrous proteins

A

Long strands of polypeptide chains - have cross-linkages due to H bonds
Insoluble
Highly repetitive sequence = strong organised structure
High proportion of hydrophobic r groups in primary structure

95
Q

What is collagen?

A

Connective tissue found in the skin, tendons, ligaments and nervous system.
Forms strong fibres and is used to provide strength

96
Q

Structure of collagen

A

3 polypeptide chains wound together in a long, rope-like structure
Therefore strong and flexible

97
Q

What is keratin?

A

Used for hard body parts - fingernails, skin, hair, horns, hooves

98
Q

Structure of keratin

A

Lots of cysteine (sulphur-containing) = lots of disulphide bonds which are strong
Strong, inflexible and insoluble
The fewer the disulphide bonds, the more flexible.

99
Q

What is elastin?

A

Found in elastic fibres (in blood vessels and alveoli) - can stretch and recoil due to coiling of elastin molecules and cross-linkages that keep the molecule together
Also found in lungs and bladder

100
Q

Structure of elastin

A

Quaternary - made from stretchy molecules (tropoelastin)

101
Q

Biological process that Ca2+ ions are involved in

A

nerve impulse transmission and muscle contraction

102
Q

Na+ ions involved in

A

nerve impulse transmission and kidney function

103
Q

K+ ions involved in

A

nerve impulse transmission and stomatal opening

104
Q

H+ ions involved in

A

pH determination and catalysis of reaction

105
Q

NH4+ ions involved in

A

production of nitrate ions by bacteria

106
Q

OH- ions involved in

A

Catalysis of reaction
Bonding between biochemical molecules
Ph determination

107
Q

NO3- ions involved in

A

present in soil and taken up by plants for amino acid and protein formation

108
Q

HCO3- ions involved in

A

Maintainence of blood pH
Works with H+ in transport of CO2 in blood

109
Q

Cl- ions involved in

A

Transport of CO2 in the blood
Moves in and out of red blood cells and maintains PH balance

110
Q

PO43- ions involved in

A

cell membrane formation and nucleic acid and ATP formation

Biology (3 decks)

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