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AQA Biology: A Level > Paper 1 and 3: Biological Molecules > Flashcards

Paper 1 and 3: Biological Molecules Flashcards

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1
Q

Monomer [definition]:

A

A molecular subunit that combines to form polymers

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2
Q

Polymer [definition]:

A

Large molecule made of smaller subunits called monomers

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3
Q

Polymerisation [2]:

A
  • The formation of polymers in an organism

- It is a condensation reaction

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4
Q

Covalent bonding[2]:

A
  • Atoms share a pair of electrons in their outer shells

- Both atoms are filled, making a more stable compound

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5
Q

Ionic Bonding [2]:

A
  • Ions with opposite charge attract one another

- The ionic bond is the electrostatic attraction between them

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6
Q

Hydrogen bonding [4]:

A
  • The electrons within a molecule are not evenly distributed but tend to spend more time at one region
  • This region becomes more negatively charged than the rest of the molecule
  • This means the molecule is polarised/ a polar molecule
  • Negative and positive regions attract each other forming a weak bond
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7
Q

Hydrogen bonds are…

A

WEAK

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8
Q

Condensation reactions [definition]:

A

Molecules react together to form a more complex molecule, a molecule of water is formed in the process

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9
Q

Hydrolysis reactions [definition]:

A

The breaking down of large molecules into smaller molecules by the addition of a water molecule

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10
Q

Metabolism [definition]:

A

All the chemical processes taking place in a living organism

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11
Q

Carbohydrates [definition]:

A

Carbon molecules combined with water

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12
Q

What elements are in carbohydrates? [3]:

A
  • Carbon
  • Hydrogen
  • Oxygen
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13
Q

Monosaccharide [definition]:

A

Monomers from which larger carbohydrates are made

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14
Q

What are some examples of common monosaccharides? [3]:

A
  • Glucose
  • Galactose
  • Fructose
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15
Q

What bond is formed in a condensation reaction between two monosaccharides?

A

A glycosidic bond

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16
Q

What are some examples of common disaccharides? [3]:

A
  • Maltose
  • Sucrose
  • Lactose
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17
Q

Maltose =

A

glucose + glucose

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18
Q

Sucrose =

A

glucose + fructose

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19
Q

Lactose =

A

glucose + galactose

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20
Q

Glucose has two isomers. What is meant by isomer?

A

Same molecular formula but different arrangement of atoms in the molecule

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21
Q

What are the isomers of glucose? [2]:

A
  • α-glucose

- β-glucose

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22
Q

For beta glucose…

A

OH is at the top

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23
Q

How are polysaccharides formed?

A

They are formed by the condensation of many glucoes units

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24
Q

Testing for reducing sugars [4]:

A
  • Add 2cm³ of the food sample to a test tube
  • If a sample is not in liquid form grind it up in water
  • Add an equal volume of benedict’s solution
  • Heat mixture in a gently boiling water bath for 5 mins
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25
Q

What is Benedict’s reagent/solution?

A

AN alkaline solution of copper (II) sulphate

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26
Q

What happens when a reducing sugar is heated with benedict’s reagent?

A

It forms an insoluble red precipitate of copper (I) oxide

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27
Q

Results in benedict’s test [2]:

A 
Positive= brick red 
negative= no colour change
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28
Q

Testing for non-reducing sugars [5]:

A
  • Use benedict’s test, if no result then proceed
  • Add 2cm³ of sample to 2cm³ of dilute hydrochloric acid in a test tube
  • Add tube to gently boiling water bath for 5 minutes
  • Slowly add some hydrogencarbonate solution to the test tube to neutralise the acid
  • Re-test using benedict’s method
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29
Q

Iodine test for starch [3]:

A
  • Place 2cm³ of the sample into a test tube
  • Add 2 drops of iodine solution and shake/stir
  • The presence of starch is indicated by a blue-black colour
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30
Q

Starch structure [5]:

A
  • Alpha glucose
  • Amylose 1-4 bonds and few 1-6 amylopectin bonds
  • A few branches in the chains of glucose
  • Chains make a helix coil
  • Insoluble
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31
Q

Starch functions and explanations [3]:

A
  • Coils make it a compact molecule, easily stored
  • Insoluble,does not affect osmotic balance
  • Branches means it is easily hydrolysed
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32
Q

Glycogen is also known as…

A

animal starch

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33
Q

Glycogen structure [4]:

A
  • Alpha glucose
  • 1-4 bonds of amylose and more 1-6 bonds of amylopectin than in starch
  • Highly branched molecule
  • Insoluble
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34
Q

Glycogen functions and explanations [3]:

A
  • Compact, can store a lot of glucose molecules in a small space
  • Chains make it easily hydrolysed
  • Insoluble, does not affect osmotic balance
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35
Q

Cellulose structure [5]:

A
  • Beta glucose
  • 1-4 bonds with amylose
  • Alternating glucose molecules by 180 degrees
  • Straight chains are unbranched
  • Microfibrils bound by hydrogen bonds
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36
Q

Cellulose functions and explanations [3]:

A
  • Makes cell wall
  • Straight chains make it strong and rigid to support the cell
  • Hydrogen bonds between chains make it strong
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37
Q

What are the characteristics of lipids? [3]:

A
  • Contain C, H, O
  • insoluble in water
  • soluble in organic solvents (alcohol, acetone)
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38
Q

What are the main groups of lipids? [2]:

A
  • Triglycerides

- Phospholipids

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39
Q

Roles of lipids [4]:

A
  • Good source of energy when oxidised
  • Insoluble in water, so waterproof
  • Slow conductors heat & electricity, so good insulators
  • Protect delicate organs
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40
Q

What are the components of triglycerides? [2]:

A
  • 3 fatty acids (tri, duh)

- Glycerol

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41
Q

Draw alpha glucose

A 
CH₂OH
   |\_\_\_\_\_\_O                  Put extra H on everything but top O
 /        .         \
OH             OH
 \                  /
   OH\_\_OH
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42
Q

How are triglycerides formed? [2]:

A
  • 3 fatty acids form an ester-bond with glycerol

- Condensation reactions

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43
Q

What causes different triglycerides to have different properties?

A

Variation in the fatty acids

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44
Q

Triglycerides [2]:

A
  • 70+ different fatty acids

- All have carboxyl group (-COOH)

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45
Q

What does it mean when a triglyceride is described as saturated? [2]:

A
  • It has no carbon-carbon double bond

- All carbons are linked to the maximum possible number of hydrogens, it is saturated with hydrogen atoms

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46
Q

What makes a triglyceride unsaturated?

A

Carbon-Carbon double bond

C=C

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47
Q

Triglyceride properties related to structure [4]:

A
  • Good energy source cus high ratio of energy-storing carbon-hydrogen bonds : carbon atoms
  • Low energy : mass makes them good storage molecules
  • Large, non-polar molecules are insoluble, no affect osmosis
  • Release a lot of water when oxidised, good water source
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48
Q

Phospholipid components [3]:

A
  • 2 fatty acids
  • Glycerol
  • phosphate group
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49
Q

Phospholipid structure and explanation [4]:

A
  • Phosphate molecules attract water forming a
  • Hydrophilic head interacts with the water but not with fat
  • Fatty acid molecules repel the water forming a
  • Hydrophobic tail orients itself away from water but mixes readily with fat
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50
Q

What does a condensation reaction form?

A

An ester bond

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51
Q

Phospholipid structure related to their properties [3]:

A
  • Polar molecule. Hydrophilic head and hydrophobic tail make it able to be in an aqueous environment
  • Hydrophilic phosphate head hold it at the surface of the cell membrane
  • Phospholipid structure allows it to form glycolipids when reacting with carbohydrates at cell membrane
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52
Q

What are glycolipids important for?

A

cell recognition at the cell-surface membrane

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53
Q

Emulsion test for lipids [4]:

A
  • Select grease-free test tube
  • Add 5cm³ of ethanol to 2cm³ of sample
  • Shake thoroughly to dissolve any lipid in the sample
  • Add 5cm³ of water and shake gently
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54
Q

Lipid test results [2]:

A
  • Lipid present = milky-white emulsion

- No lipid = should remain clear

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55
Q

Amino acid [definition]:

A

The basic monomer units which combine to make a polypeptide

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56
Q

Amino acid structure [5]:

A
  • Central carbon
  • Amine group (-NH₂)
  • Carboxyl group (-COOH)
  • Hydrogen atom (-H)
  • R group
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57
Q

The formation of a peptide bond [3]:

A
  • The -OH from one carboxyl group bonds with the H from the other amino acid
  • This is a condensation reaction that forms a molecule of water
  • A peptide bond is formed between the carbon atom of one amino acid and the Nitrogen atom of the other
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58
Q

The primary structure of proteins:

A

The sequence of amino acids in a polypeptide chain

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59
Q

The secondary structure proteins:

A

α-helices and β-pleated sheets

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60
Q

What causes the secondary structure of proteins? [2]:

A
  • Form as a result of hydrogen bonding between different amino acid chains.
  • Hydrogen bonds can form between the amine and carboxyl groups or amine and hydroxyl groups
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61
Q

Tertiary structure of proteins [2]:

A
  • The 3D structure of protein

- Bonds in tertiary structure depend on the primary structure primary structure

62
Q

Bonds in tertiary structure of protein [3]:

A
  • Disulfide bridges
  • Ionic bonds
  • Hydrogen bonds
63
Q

Disulfide bridges in tertiary structure [2]:

A
  • Fairly strong bonds

- Not easily broken

64
Q

Ionic bonds in tertiary structure [3]:

A
  • Formed between carboxyl group and amino acid
  • Weaker than disulfide bonds
  • Easily broken by changes in pH
65
Q

Hydrogen bonds in tertiary structure;

A

Numerous but easily broken

66
Q

Quaternary structure of protein;

A

The association of several protein chains or subunits into a closely packed arrangement

67
Q

How are dipeptides formed?

A

By condensing 2 amino acids

68
Q

How are polypeptides formed?

A

By condensing many amino acids

69
Q

Functional proteins may contain one or more…

A

polypeptide

70
Q

The biuret test for proteins [3]:

A
  • Place sample in a test tube
  • Add an equal volume sodium hydroxide solution
  • Add a few drops of dilute copper (II) solution and mix gently
71
Q

Protein test results [2]:

A
  • positive (peptide bond present) = violet

- negative = solution stays blue

72
Q

What is the function of proteins? [4]:

A
  • Repairs and builds your body’s tissues
  • Enzymes are proteins
  • Antibodies are proteins
  • Proteins are a major class of hormones
73
Q

Enzyme [definition]:

A

Globular proteins that are biological catalysts that speed up the rate of a chemical reaction without getting used up

74
Q

Fibrous proteins [4]:

A
  • They form long chains or fibres
  • They have primary, secondary, tertiary and quaternary structures
  • Fibrous nature makes them insoluble in water which makes them useful for structure and support
  • Fibres form a triple-helix of polypeptide chains. These chains are held together by hydrogen bonds
75
Q

How do enzymes catalyse reactions? [2]:

A
  • They lower the activation energy by creating a different reaction pathway.
  • This increases the number of successful collisions = more enzyme-substrate complexes
76
Q

Active site [2]:

A
  • Made up of a relatively small number of amino acids

- It forms a small depression within the much larger enzyme

77
Q

Substrate [definition]:

A

The molecule on which the enzyme acts

78
Q

The properties of an enzyme relate to…

A

the tertiary structure of its active site and its ability to combine with complementary substrate to form an enzyme-substrate complex

79
Q

Specificity of enzymes;

A

Enzymes are specific and complimentary to the substrate

80
Q

Lock and key model [2]:

A
  • The active site fits perfectly with the substrate

- The binding of the substrate to the active site is a rigid interaction

81
Q

The induced fit model [3]:

A
  • The active site forms as the enzyme and substrate interact
  • The proximity of the substrate leads to a change in the enzyme which forms a functional active site
  • The enzyme is flexible and can mould itself around the substrate
82
Q

Factors that affect enzyme action [5]:

A
  • Temperature
  • pH
  • Enzyme concentration
  • Substrate concentration
  • Inhibitors
83
Q

Temperature’s effect on enzyme activity [4]:

A
  • More effective collisions resulting in more enzyme-substrate complexes being formed
  • The rate of reaction increases
  • Hydrogen bonds in enzyme begin to break
  • This results in the active site changing shape/ denaturing (ROR begins to plateau)
84
Q

Effect of pH on enzyme action [3]:

A
  • A Change in pH alters the charges of the amino acids that make up the enzyme active site
  • Substrate can no longer become attached to the active site (enzyme-substrate complexes cannot be formed)
  • If there is a significant change in pH the bonds maintaining the enzyme’s tertiary structure break, causing the active site to change shape
85
Q

What is the pH a measure of?

A

A solution’s hydrogen ion concentration

86
Q

Effect of enzyme concentration on the rate of reaction [2]:

A
  • As long as there is an excess of substrate the increase of enzyme leads to an increase in the ROR
  • If the substrate is limiting then an increase in enzyme will have no effect on the rate of reaction
87
Q

Effects of substrate concentration on the rate of reaction [2]:

A
  • If the enzyme concentration is fixed and substrate concentration is slowly increased the ROR increases in proportion to the substrate increase
  • This is because there are many substrates for the enzyme to react with creating more enzyme-substrate complexes
88
Q

Competitive inhibitors [4]:

A
  • They have a molecular shape similar to that of the substrate
  • This allows them to occupy the active site of the enzyme
  • They compete with the substrates for available active sites
  • The inhibitor is not permanently bound to the active site, which means all substrate molecules will eventually occupy an active site
89
Q

Non-competitive inhibitors [3]:

A
  • They attach themselves to the enzyme at a binding site which is NOT the active site
  • Upon attaching to the enzyme the inhibitor alters the shape of the enzyme and thus the active site
  • As the substrate and inhibitor are not competing for the same site increasing the substrate concentration does not decrease the effect of the inhibitor
90
Q

What does DNA stand for?

A

Deoxyribonucleic acid

91
Q

Nucleotide structure [3]:

A
  • A pentose sugar
  • A phosphate group
  • Nitrogen-containing organic base
92
Q

What are the nitrogen-containing organic bases? [5]:

A
  • Cytosine (C)
  • Guanine (G)
  • Thymine (T)
  • Adenine (A)
  • Uracil (U)
93
Q

The nitrogen bases are…

A

specific and complimentary

94
Q

What does A pair up with in DNA?

A

T

95
Q

What does A pair up with in RNA?

A

U

96
Q

What does C pair up with?

A

G

97
Q

What does G pair up with?

A

C

98
Q

What does T pair up with?

A

A

99
Q

What are the components of DNA [3]:

A
  • Deoxyribose sugar
  • Organic nitrogen base
  • Phosphate
100
Q

What is the nitrogen and carbon containing molecule comprising a two ring structure?

A

Purine

101
Q

What is the nitrogen and carbon containing molecule comprising a one ring structure?

A

Pyrimidine

102
Q

What are the weak bonds formed between complementary bases?

A

Hydrogen bonds

103
Q

What is the arrangement of complimentary polynucleotides in the double helix?

A

Antiparallel in a clockwise direction

104
Q

What are the strong bonds formed between adjacent nucleotides in a polynucleotide?

A

Phosphodiester bonds

105
Q

What is the number of hydrogen bonds between adenine and thymine?

A

2

106
Q

What is the number of hydrogen bonds between cytosine and guanine?

A

3

107
Q

DNA function [2]:

A
  • DNA is an important information-carrying molecules.

- In all living cells, DNA holds genetic information and passes it from generation to generation

108
Q

DNA structure [2]:

A
  • Specific and complementary base pairing

- Double helix (2 polynucleotide chains being twisted)

109
Q

The history of DNA:

A
  • In 1953 James Watson and Francis Crick discovered the structure of DNA, following Rosalind Franklin’s work on the x-ray
110
Q

Pyrimidine bases [2]:

A
  • Thymine

- Cytosine

111
Q

Purine bases [2]:

A
  • Adenine

- Guanine

112
Q

What is the bond between two mononucleotides?

A

Phosphodiester bonds

113
Q

RNA components [3]:

A
  • Ribose sugar
  • Phosphate group
  • Nitrogen-containing organic bases
114
Q

What replaces thymine in RNA strands?

A

Uracil

115
Q

What is the function of RNA? [3]:

A
  • mRNA molecules carry the coding sequences for protein synthesis and are called transcripts
  • rRNA molecules form the core of a cell’s ribosomes
  • tRNA molecules carry amino acids to the ribosomes during protein-synthesis
116
Q

RNA structure [2]:

A
  • It is a single, relatively short, polynucleotide chain

- has uracil instead of thymine

117
Q

How is DNA adapted to suit its function? [3]:

A
  • Very stable molecule, passes from generation to generation without significant change
  • Base pairing leads to DNA being able to replicate and transfer info as mRNA
  • Two polynucleotide strands joined by hydrogen bonds, allows them to separate during DNA replication
118
Q

What are the requirements for semi-conservative DNA replication to take place? [4]:

A
  • Enzyme DNA polymerase
  • the four types of bases with their pairs
  • Chemical energy source
  • Both strands of DNA to act as a template
119
Q

Semi-conservative DNA replication ensures…

A

genetic continuity between generations of cells.

120
Q

Erwin Chargaff [2]:

A
  • Base pairings rule

- Ratio of base pairs is specific to the species

121
Q

Semi-conservative replication [5]:

A
  • Enzyme DNA helicase breaks down hydrogen bonds that link base pairs of DNA
  • Double helix strands unwind
  • Polynucleotide strands then act as a template for free base pairs to bind to
  • Nucleotides are held together by the condensation of the DNA polymerase to form missing polynucleotide
  • Each new dna molecule contains one of the original strands
122
Q

What does ATP stand for?

A

Adenosine triphosphate

123
Q

Components of ATP [3]:

A
  • Adenine
  • Ribose sugar
  • 3 Phosphate groups
124
Q

What enzyme catalyses the hydrolysis of ATP to adenosine diphosphate (ADP) and an inorganic phosphate group (Pi) ?

A

ATP hydrolase

125
Q

Hydrolysis of ATP [2]:

A
  • The hydrolysis of ATP can be coupled to energy-requiring reactions within cells.
  • The inorganic phosphate released during the hydrolysis of ATP can be used to phosphorylate other compounds, often making them more reactive.
126
Q

ATP is re-synthesised [2]:

A
  • Re-synthesised by the condensation of ADP and Pi.

- This reaction is catalysed by the enzyme ATP synthase during photosynthesis, or during respiration

127
Q

Properties of water [5]:

A
  • Metabolite
  • Solvent
  • Temperature control
  • Cohesion
  • Surface tension
128
Q

Water as a metabolite;

A

metabolite in many metabolic reactions, including

condensation and hydrolysis reactions

129
Q

Water as a solvent;

A

Its an important solvent in which metabolic reactions occur

130
Q

Cohesion in water molecules [2]:

A
  • Water molecules ‘stick’ together. This helps transport water in plants and other organisms
  • Water cohesion leads to surface tension
131
Q

Temperature control in water [4]:

A
  • Has a high latent heat of vaporization
  • High specific heat capacity
  • This water in and around our cells absorbs a lot of heat energy without its temperature increasing much.
  • The water ‘buffers’ the heat change
132
Q

Surface tension in water [3]:

A
  • Because of its hydrogen bonds, water has a high surface tension
  • Makes water behave as if there is a skin where the water meets air.
  • This allows small animals to live on the surface of water bodies
133
Q

Where are inorganic ions found?

A

Inorganic ion occur in cytoplasm and bodily fluids, some in high concentration and some in low concentration

134
Q

Sodium ions [2]:

A
  • Na⁺

- Important in helping other molecules move across membranes (co-transport)

135
Q

Iron ions [2]:

A
  • Fe²⁺, Fe ³⁺

- Important in haemoglobin, cus they carry oxygen

136
Q

Phosphate ions [3]:

A
  • PO₄³⁻
  • Used in ATP (atp contains phosphate groups)
  • RNA & DNA have reactions with phosphate groups to form polynucleotides
137
Q

Ester bonds =

A

Between fatty acid and glycerol

138
Q

Glycosidic bonds=

A

Between carbohydrates

139
Q

DNA transcription step 1

A

DNA helicase moves along the strand breaking H bonds btwn complementary bases, to separate the strands

140
Q

DNA transcription step 2

A

mRNA polymerase moves along, joining free RNA nucleotides to DNA template via complementary base pairing

141
Q

DNA transcription step 3

A

Phosphodiester bonds form between RNA nucleotides by condensation reaction

142
Q

DNA transcription step 4

A

Splicing of pre-RNA

143
Q

DNA transcription step 5

A

Hydrogen bonds reform btwn complementary bases

144
Q

DNA translation step 1

A

mRNA attaches to ribosomes

145
Q

DNA translation step 2

A

mRNA has a codon (triplet bases that determine amino acid sequence)

146
Q

DNA translation step 3

A

tRNA binds to complementary anticodon cus complementary base pairing (a-u c-g)

147
Q

DNA translation step 4

A

A 2nd trna with complimentary anticodon binds to 2nd codon on mrna by complementary base pairing

148
Q

DNA translation step 5

A

Peptide bond forms btwn 2 aminoacids by condensation reaction (energy is required)

149
Q

DNA translation step 6

A

1st tRNA is removed & process repeats until it reaches a stop codon

150
Q

Where does the protein go after translation?

A

To the rough endoplasmic reticulum

AQA Biology: A Level (18 decks)

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