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CIE Biology A1 > Biological molecules > Flashcards

Biological molecules Flashcards

carbohydrates lipids proteins nucleic acids

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1
Q

macromolecule definition and examples

A

giant molecule, eg. Proteins, Carbohydrates, Nucleic acids

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2
Q

organic molecule definition

A

molecules containing carbon and hydrogen

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3
Q

natural polymers and the monomers they are made out of

A

polysaccharides (monosaccharides and disaccharides)
proteins (amino acids)
nucleic acids (nucleotides)
NOT LIPIDS

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4
Q

manmade polymers

A

PVC, nylon, polyester, polythene

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5
Q

General formula of carbohydrates

A

Cx(H2O)y

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6
Q

elements in carbohydrates

A

Carbon
hydrogen
oxygen

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7
Q

monosaccharides examples

A

glucose
fructose
galactose

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8
Q

uses of monosaccharides

A

energy and respiration (broken bonds transfer energy for ATP)
building blocks for larger molecules

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9
Q

characteristics of monosaccharides

A

sweet, water soluble, single molecules CH20n

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10
Q

glucose formula

A

C6H12O6

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11
Q

isomers

A

Molecules of the same molecular formula with diferent structural formulae.

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12
Q

alpha glucose positioning of hydroxyl groups

A

down, down, up, down (right to left)

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13
Q

beta positioning of hydroxyl groups

A

up, down, up down (right to left)

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14
Q

Disaccharides

A

2 monosaccharides joined together

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15
Q

sucrose monomers

A

a glucose + b fructose

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16
Q

maltose monosaccharides

A

a glucose + a glucose

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17
Q

lactose monosaccharides

A

b galactose + b glucose

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18
Q

Where do you start numbering carbon atoms?

A

From the end with a double bond to oxygen

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19
Q

Structure of pentoses and hexoses

A

ring structure with carbon 1 bonded to carbon 5 so that carbon 6 is isolated from the ring.

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20
Q

How are disaccharides formed?

A

via a condensation reaction forming a glycosidic bond between the 2 monosaccharides and releasing a water molecule.

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21
Q

disadvantages of qualitative biological molecules tests

A

cant be quantified to give exact concentrations or types of molecules.

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22
Q

protein test

A

biuret solution heated w sample and turns from blue to purple.

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23
Q

starch test

A

iodine turns starch black

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24
Q

lipids test

A

mix ethanol with solution and add water to turn cloudy

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25
Q

reducing sugars

A

sugars with an aldehyde/ketone/hydroxyl group so therefore acts as an oxidising agent.

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26
Q

test for reducing sugars

A

add benedicts solution to sample in water bath and will turn brick red

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27
Q

test for non reducing sugars

A

sample is boiled and HCl is added to it (hydrolysis via acidification) before cooling and adding benedicts reagent.

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28
Q

colorimeter

A

measures a solutions absorbance of specific wave lengths to create a calibration curve at 735nm.

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29
Q

proteins function

A

structure and functioning of cell for transport and movement, eg centrioles

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30
Q

inorganic ion function

A

participate in metabolic reactions. eg chlorophyll has aluminium

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31
Q

water function

A

metabolic processes, fluid pressure, temp control and solvent.

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32
Q

nucleotides and nucleic acids function

A

coding of cell, construction and functioning. ATP is derivative of nucleotide

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33
Q

carbohydrates

A

structure, energy storage and cellular recognition

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34
Q

lipids function

A

energy storage and cellular membrane

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35
Q

organic macromolecule groups

A

carbs, lipids, proteins, nucleic ACIDS

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36
Q

CARB elements and monomer

A

sugars

CHO

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37
Q

protein monomer and elements

A

amino acids

C H O N S

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38
Q

lipids monomer and elements

A

ISNT A POLYMER

C H O

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39
Q

nucleic acids monomer and elements

A

nucleotides

C H O N P

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40
Q

reactions that split disaccharides and polysaccharides

A

hydrolysis using hydrogen and a hydroxyl group, catalysed by specific enzymes

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41
Q

functional properties of polysaccharides depend on?

A

composition and isomers involved

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42
Q

polysaccharides

A

macromolecules consisting of straight/branched chains of monosaccharides, eg starch, cellulose, glycogen

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43
Q

cellulose,
where’s it found?
structure?
what’s it made of? bonding?

A

cell walls of plants
unbranched
beta glucose molecules joined by stable 1,4 glycosidic links
produces parallel chains which are cross linked w hydrogen bonds to form microfibrils

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44
Q

microfibrils

properties

A

cross linked hydrogen bonded chains of cellulose.
strong, provide cell wall w strength and rigidity
40-70 cellulose chains

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45
Q

starch
what’s it made of?
structure?
function?

A

long chains of alpha glucose linked together w 25-30% amylose and 70-75% amylopectin
energy storage
amyloplasts in plants to be hydrolysed by enzymes as an energy source when required

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46
Q

amylose structure

A

linear, helical, unbranched a glucose chains linked via 1,4 glycosidic bonds
every turn requiring six a glucose molecules
25-30% structure of starch

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47
Q

amylopectin structure and composition

A

branched chains of 1,6 glycosidic bonds every 24-30 glucose units
1,6 provide branching points
allows millions of molecules to be joined in a compact form.

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48
Q

glycogen
structure?
composition?
properties?

A

branched polysaccharide composed of a glucose molecules
glycosidically linked via 1,6 and 1,4
more highly branched and water soluble than starch
storage compound in animal tissues

49
Q

amyloplasts

A

non-pigmented storage organelles within plant cells

50
Q

Why is amylopectin less soluble than glycogen?

A

because it has less 1,6 glycosidic links w 1,4 links so is less soluble

51
Q

lipids

A

non-polar, hydrophobic organic molecules made up of fatty acids, classified as saturated/unsaturated fatty acids.
eg fats, waxes, sterols and phospholipids

52
Q

why do lipids not dissolve in water?

A

hydrophobic so repel water molecules

53
Q

fatty acid composition

A

even number of carbon atoms with hydrogen bound along the chain length, carboxyl group at end forms an acid.

54
Q

neutral fats

A

form fats and oils in plants and animals, consisting of a glycerol attached to one (mono), two (di) or three (tri) fatty acids via ester bonds

55
Q

why are lipids good at storing energy?

A

metabolism of the molecule releases chemical energy from hydrogen present in fatty acid chains. Are v reduced and anhydrous, meaning provide much energy for small stores.

56
Q

saturated fatty acids

A

contain maximum number of hydrogen atoms

57
Q

unsaturated fatty acids

A

contain double bonds between carbons

58
Q

monounsaturated

A

containing only one double bond

59
Q

polyunsaturated

A

containing two or more double bonds

60
Q

how does proportions of saturated fatty acids affect the state of a molecule?
why?

A

higher proportion leads to a more solid state
however higher proportion of unsaturated leads to a liquid state at rtp.
unsaturation causes kinks so chains don’t pack as closely together

61
Q

formation of triglycerides

A

condensation reaction between glycerol and 3 fatty acids.

ester bond is formed between the glycerol hydroxyl group and a hydrogen off of a fatty acid, releasing a water molecule.

62
Q

glycerol

A

an alcohol with 3 carbons bonded to a hydroxyl group.

63
Q

esterification

A

condensation reaction of an alcohol with an acid with an acid, forming an ester and water.

64
Q

lipolysis

A

breakdown of lipids involving hydrolysis of triglycerides into glycerol molecules and fatty acids.

65
Q

biological functions of lipids

A 
concentrated sources of energy, fuel for respiration
structure of cell membranes
waterproofing in plants and animals
shock absorbers for protection
source of metabolic water
insulation
66
Q

phospholipids

A

modified triglycerides in which a phosphate group replaces the fatty acid

67
Q

phosphate ion

A

PO43-

68
Q

hydrophilic end of the phospholipid

A

phosphate end of the molecule

69
Q

hydrophobic end of a phospholipid

A

fatty acid end repels water molecules

70
Q

phospholipid bilayer

A

when the hydrophilic phosphate end of a phospholipid turns inwards towards the water and hydrophobic turns away, forming a bilayer.

71
Q

amphipathic

A

having hydrophobic and hydrophilic ends

72
Q

structure of saturated vs unsaturated fatty acid tails

A

unsaturated forms kinks and saturated forms straight chains.

greater number of double bonds increases the fluidity of the membrane.

73
Q

amino acid formation

A

join together in condensation reactions in a linear chain to form polypeptides, sequence defined by a gene and encoded in the genetic code.
they also are joined via peptide bonds to form long polypeptide chains

74
Q

how are genes broken down?

A

in the presence of water, they break down via hydrolysis into their constituent amino acids.

75
Q

what’s a nucleotide made up of?

A

one carbon joined to a hydrogen, amine group (NH2), carboxyl group and chemically variable ‘r’ group

76
Q

whats different in each type of amino acid?

A

the R group determines interactions with other amino acids and therefore how it folds up into a functional protein.

77
Q

cysteine

A

forms disulphide bridges with other cysteine amino acids to form cross links in a polypeptide chain.

78
Q

lysine

A

r group donating an alkaline property

79
Q

aspartic acid

A

donates acidic property

80
Q

where do peptide bonds form between amino acids?

A

between the carboxyl group of one and the amine group of another, forming water

81
Q

primary structure

A

the sequence of amino acids in a polypeptide

82
Q

what determines the primary structure?

A

the order of nucleotides in DNA and mRNA

83
Q

what determines the secondary structure of proteins?

A

the composition and position of amino acids along with hydrogen bonding between amino acids.

84
Q

What determines tertiary structure

A

Interaction between R groups

85
Q

Tertiary structure

A

A three dimensional shape held by ionic bonds and disulphide bridges

86
Q

Channel proteins

A

Proteins that fold to form channels in the plasma membrane.
Non-Polar R groups face the membrane and polar face the inside of the channel so hydrophilic molecules pass and ions pass through into the cell.

87
Q

Enzymes

A

Globular proteins that catalyse reactions.
Polar active sites specific to polar substances
Non polar specific to non polar substances

88
Q

Sub-unit proteins

A

Consist of two or more subunits in a complex quarternary structure.

89
Q

Denaturation

A

When chemical bonds holding a protein break and can’t hold its 3 dimensional shape so can’t carry out biological function.

90
Q

Causes of denaturation

A

pH

Heat

91
Q

Proteins

A

Complex macromolecules built up from linear sequence of units of amino acids

92
Q

Primary structure

A

Amino acid sequence linked via peptide bonds to form giant polypeptide chains organised by attractive and repulsive charges on amino acids.

93
Q

Secondary structures

A

Alpha helix or beta pleated sheet

Maintained by hydrogen bonds between neighbouring CO and NH groups (collectively strong).

94
Q

Alpha helix

A

Hydrogen bonds collectively strong, joining amino acids.

95
Q

Beta pleated sheet

A

Formed via 2 peptide chains joined via hydrogen bonds.

96
Q

Tertiary structure

A

3 dimensional shape formed in folding of secondary structures via disulphides bonds between cysteine amino acids, ionic bonds and hydrogen bonds as well as hydrophobic interactions.

97
Q

How are tertiary structures broken?

A

Heavy metals
Solvents
pH and temp extremes

98
Q

Quarternary structure

A

Arrangement of the polypeptide chains into a functional protein.

99
Q

Globular protein properties

A

Water soluble
Necessary tertiary structure
Polypeptide chains folded

100
Q

Globular proteins function

A

Catalytic eg enzymes
Regulatory eg insulin
Transport eg haemoglobin
Protection eg antibodies

101
Q

Haemoglobin

A

Oxygen transporting protein in red blood cells, consisting of 4 polypeptide chains (2 alpha and 2 beta).
Each subunit contains a non-protein prosthetic group and ahem group (w Fe) which binds to oxygen.

102
Q

Insulin

A

Peptide hormone composed of 2 peptide chains (A and B) linked via 2 diulfide bonds.

103
Q

RuBisCo

A

Multi-unit enzyme found in green plants catalysing carbon fixation in the Calvin cycle, consisting of 8 large and 8 small subunits arranged as 4 dimers.

104
Q

Properties of fibrous proteins

A

Water insoluble
Tough (stretchy)
Long fibres/sheets

105
Q

Function of fibrous proteins

A

Structural

Contractile

106
Q

Collagen structure

A

3 polypeptides wound via hydrogen bonds to form a helical rope with every third amino acid as a glycine.
Self assemble into fibrils by covalent cross linkages, bundling to form fibres.

107
Q

Collagen function

A

Component of connective tissue, mostly found in fibrous tissues.

108
Q

Keratin

A

Polypeptide chains arranged in parallel sheets held together by hydrogen bonds.

109
Q

Polarity of water

How does this affect it?

A

Oxygen has slight negative chart while hydrogen have slight positive.
Means weak hydrogen bonds are formed between each molecule. Also affects intermolecular forces between other polar molecules, allowing ions to stay dissolved in water.

110
Q

Water functions

A

Provides medium in which metabolic reactions occur (also able to act as base/acid).
Provides an aquatic environment due to high heat capacity, keeping large bodies of water thermally stable.

111
Q

Water properties

A

Cohesive
Adhesive
Solvent
Thermal

112
Q

Cohesive property of water

A

Stick together due to hydrogen bonds formed between each molecule, allowing development of surface tension.

113
Q

Adhesive property of water

A

Attracted to other molecules as forms hydrogen bonds between other polar molecules.

114
Q

Solvent property of water

A

Dipolar nature allows it to surround other charged molecules and prevent them clumping.

115
Q

Thermal properties of water

A

Highest heat capacity so forms thermally stable bodies of water.
High bp as much energy is needed to break the H bonds, supporting life and metabolic processes.
High latent heat of vaporisation, meaning sweat has cooling effect.

116
Q

Water solvent properties in the wild

A

Dissolved minerals are available to aquatic organisms.

Blood plasma transports many substances.

117
Q

Thermal properties of water in wild

A

Allows temp sensitive metabolic processes to take place in organisms

118
Q

water role in cells

A

main component and provides an aqueous environment for metabolic reactions to occur

CIE Biology A1 (15 decks)

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