AS Topic 2 Flashcards

1
Q

Why are cell membranes vital structures?

A

They create an enclosed space separating the internal cell environment from the external cell environment

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2
Q

What does a cell membrane consist of?

A

Phospholipid bilayer containing proteins, cholesterol, glycoproteins and glycolipids

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3
Q

What are phospholipids made up of?

A

a molecule of glycerol
a polar hydrophilic phosphate group (head)
2 non polar hydrophobic fatty acid tails (lipid tail)

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4
Q

How do the phospholipids contribute to the structure of the cell membrane?

A

Due to the hydrophilic phosphate head of the molecule, it attracts other polar molecules like water. The fatty acid tails are non polar and are therefore hydrophobic, this means the phospholipids become arranged so the tails have no contact with the water.

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5
Q

What does the term ‘fluid mosaic’ mean in reference to cell membranes?

A

The bilayer is fluid as particles are always constantly moving
Different types of protein are scattered through the bilayer like a mosaic

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6
Q

What are models of membrane structure?

A

Interpretations of data which can change when scientific advances enable new discoveries. Models represent real life structures and processes

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7
Q

What is the role of proteins within the cell membrane?

A

Involved with cell transport and communication

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8
Q

What is the difference between glycolipids and glycoproteins?

A

Glycolipids - lipids with carbohydrate attached

Glycoproteins - proteins with carbohydrate attached and are longer than glycolipids, makes the membrane more rigid

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9
Q

What is the difference between intrinsic and extrinisic proteins?

A

Intrinsic/integral - embedded within the membrane, precise arrangement determined by hydrophillic and hydrophobic regions
Extrinsic/peripheral - attatched to the outer or inner surface of the membrane

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10
Q

What is the location and function of glycolipids and glycoproteins in the cell membrane?

A

Location: present on surface of cell membrane

Function: aid cell to cell communication by attaching as cell markers or binding with substances at the cell surface

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11
Q

What is the role of cholesterol within the cell membrane?

A

Found between the phospholipids where it regulates membrane fluidity by stopping the phospholipid tails from packing too closely together

It increases the mechanical strength and stability of membranes (at higher temps too) and without it membranes would break down and cells would burst

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12
Q

What are the properties of gas exchange surfaces?

A

-surface area to volume ratio
-diffusion pathway
-concentration gradient

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13
Q

How does surface area to volume ratio affect different organism exchange systems?

A

As organisms increase in size, their SA:Vol ratio decreases.

This means there is a longer distance for diffusion, so larger multicellular organisms have evolved adaptation to facilitate the exchange of substances (e.g. alveoli in mammals, gills in fish)

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14
Q

What is Fick’s Law?

A
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15
Q

What does Fick’s law predict the rate of diffusion to be

A

This means that diffusion rate will double if surface area or concentration gradient increases/diffusion pathway halves

Or if the thickness halves

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16
Q

How does Fick’s law explain the adaptation of mammalian gas exchange surfaces?

A
  1. rate of diffusion proportional to surface area - (alveoli have large surface area)
  2. rate of diffusion proportional to difference in conc - (breathing and constant blood flow maintains steep concentration gradient)
  3. rate of diffusion inversely proportional to thickness of exchange surface - (walls of alveoli/capillaries one cell thick)
  4. diffusion distance shortened due to flattened cells forming alveoli and capillary walls
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17
Q

What are the adaptations of the mammalian lung?

A

-cilia hair in trachea wafts mucus, which traps dust and pathogens
-bronchioles have smooth muscles and elastic fibres to allow adjustment of size of airway
-ALVEOLI

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18
Q

How are the alveoli adapted for efficient gas exchange?

A

Good blood supply creates a steep concentration gradient, alveolar wall and capillary wall are only 1 cell thick, layer of moisture lines alveoli so O2 and CO2 dissolve and exchange occurs in solution

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19
Q

What is diffusion?

A

The net movement of particles from an area of high concentration to an area of low concentration going down the concentration gradient

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20
Q

When does diffusion occur, and when does it stop?

A

Wherever there is a concentration gradient, and Diffusion will continue until equilibrium is reached

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21
Q

What are the properties of molecules that move by simple diffusion?

A

Small (can fit between phospholipids)

Non-polar (can interact with hydrophobic non polar tails)

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22
Q

What molecules require facilitated diffusion, and why?

A

Large, polar molecules (cannot fit through phospholipid bilayer and cannot pass through hydrophobic tails)
Ions

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23
Q

What is facilitated diffusion?

A

Facilitated diffusion is the passive movement of larger/polar molecules across a membrane, from a region of high concentration to a region of low concentration via protein channels

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24
Q

What is a carrier protein?

A

A transmembrane protein that switches shapes when the ion or molecule binds onto a specific site on the protein, as a result of change in shape, the ion or molecules crosses the membrane (direction dependent on concentration gradient)

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25
Q

What is a channel protein?

A

Pores that extend from one side of the membrane to the other, allowing charged substances to diffuse through. Have a FIXED SHAPE

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26
Q

What is passive transport?

A

No metabolic energy required for the transport, driven by concentration gradient.

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27
Q

what are the steps of facilitated diffusion through a carrier protein

A
  1. First a large molecule attaches to a carrier protein in the membrane
  2. The protein changes shape
  3. This releases the molecule on the opposite side of the membrane
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28
Q

What is osmosis?

A

the net movement of water particles from an area of high water potential to an area of low water potential through a partially permeable membrane

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29
Q

How does the partial permeability of the surface membrane of the cells allow osmosis to take place?

A

Is a barrier to some solutes, but not water. Enables a concentration gradient of solutes/water

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30
Q

What happens when water moves into a cell via osmosis? (animal vs plant)

A

Animal cell - can burst

Plant cell - cell wall prevents bursting

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31
Q

What happens when water moves out of a cell via osmosis? (animal vs plant)

A

Animal cell - shrivels

Plant cell - vacuole and cytoplasm shrink away from the cell wall

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32
Q

What is active transport?

A

The movement of a substance against a concentration gradient, requiring ATP and a CARRIER protein

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33
Q

What are some examples of active transport?

A

Reabsorption of useful molecules and ions into the blood after filtration into the kidney tubules
Loading inorganic ions from the soil into root hair cells

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34
Q

When does active transport occur

A

Occurs when diffusion cannot meet needs of cell quick enough or if against concentration gradient

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35
Q

Process of active transport broken down

A

→ Shape of carrier protein is complementary to molecule they carry
→ binding
→ ATP hydrolysed - ADP + P (energy released)
→ carrier protein changes shape
→ molecule transported across membrane
→ 1 way flow molecule can only fit into carrier protein on 1 side of the membrane (ensures low to high concentration)

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36
Q

What is exocytosis?

A

Exocytosis is the release of substances, usually proteins or polysaccharides, from the cell

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37
Q

How does exocytosis occur, and what is an example of this?

A

Vesicles containing substance pinch off from sacs of Golgi apparatus, move towards and fuse with the cell surface membrane to be released outside of the cell. ACTIVE PROCESS

Example - insulin released into blood by exocytosis

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38
Q

What is endocytosis?

A

Endocytosis is taking in substances from outside the cell

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39
Q

How does endocytosis occur, and what is an example of this?

A

A cell can surround a substance with a section of its cell membrane where it then pinches off to form a vesicle inside the cell containing the ingested substance ACTIVE PROCESS

Example - white blood cells ingesting bacteria (phagocytosis)

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40
Q

What are proteins

A

long chains of peptide molecules e.g. amino acids

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41
Q

What are amino acids?

A

Monomers of polypeptides

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42
Q

How do amino acids form polypeptides?

A

Peptide bonds form between amino acids, these are covalent bonds formed via condensation reactions (loss of water molecule)

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43
Q

What is the chemical structure of an amino acid

A

Amino acids contain an amino group (-NH2), a carboxyl group (-COOH) and a carbon containing R group (also known as the variable side group)

They all have the same general structure: a central carbon atom bonded to an amine group, a carboxyl group, a hydrogen and a residual group

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44
Q

What is primary structure?

A

The sequence of amino acids in the polypeptide chain, bonded by covalent peptide bonds. This is specific for each protein

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45
Q

What is secondary structure?

A

Hydrogen bonds forming between weak, negatively charged nitrogen and positively charged hydrogen atoms creating either an a helix or B pleated sheet

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46
Q

What is an α helix and how does it form?

A

The α-helix shape occurs when the hydrogen bonds form between every fourth peptide bond (between the negative oxygen of the carboxyl group and the positive hydrogen of the amine group)

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47
Q

What is a β-pleated sheet and how does it form?

A

The β-pleated sheet shape forms when the protein folds so that two parts of the polypeptide chain are parallel to each other enabling hydrogen bonds to form between parallel peptide bonds

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48
Q

What is tertiary structure?

A

The three dimensional arrangement of the polypeptide chain in space, brought about by additional bonds (hydrogen, ionic, disulphide, weak hydrophobic interactions) between R groups

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49
Q

What is quaternary structure?

A

Occurs in proteins that have more than one polypeptide chain working together, same bonds responsible for tertiary structure

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50
Q

What is the structure of globular proteins?

A

Polypeptide chain folded into compact spherical shape. Non polar hydrophobic regions orientated towards the centre of the protein (away from aqueous surroundings), polar hydrophilic groups orientate themselves on outside of protein
3D shape critical in role of binding to other substances
Tertiary and potentially quaternary structure

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51
Q

Why are globular proteins soluble

A

Proteins soluble - water molecules surround polar hydrophilic R groups + easily transported in fluids due to hydrophilic side chains that interact with water molecules hydrophobic amino acids hide deep within the protein well away from water

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52
Q

What are the properties of globular proteins?

A

They are water soluble due to the hydrophillic side chains that project from outside the molecule.
Mostly involved in physiological roles

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53
Q

What is the structure of fibrous proteins?

A

Long strands of polypeptide chains with cross linkages due to hydrogen bonds. Little/no tertiary structure.

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54
Q

What are the properties of fibrous proteins?

A

Insoluble due to hydrophobic R groups on the outside.

Mainly involved in structural and support roles

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55
Q

What are the similarities between globular and fibrous proteins?

A

They both are chains of amino acids joined by peptide bonds

They both are joined by named bonds (e.g. hydrogen, ionic, disulphide)

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56
Q

What are some examples of globular and fibrous proteins?

A

Globular - haemoglobin

Fibrous - collagen and keratin

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57
Q

Structure of haemogloblin

A

globular protein made up of 4 polypeptide chains

Has iron-containing prosthetic haem (Fe2+) groups that bind to oxygen which releases when required forming oxyhaemoglobin
4 sub units and a haem group, four oxygen molecules = 8 oxygen atoms

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58
Q

Functions of a haemogloblin

A

carries oxygen around the body in blood due to its solubility

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59
Q

Structural and functional differences of globular and fibrous proteins

A

Fibrous proteins straight chains globular compact and spherical
Globular soluble fibrous not
Fibrous involved in structural functions globular isn’t
Globular involved in catalysis as enzyme fibrous not

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60
Q

Differences between collagen and Haemogloblin

A
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61
Q

How is transcription involved in the synthesis of an enzyme?

A

DNA strand unwinds in nucleus and hydrogen bonds between bases are broken. Antisense strand is used for mRNA synthesis, RNA polymerase links RNA nucleotides. Complementary base pairing of A with U on RNA rather than T

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62
Q

What is an enzyme?

A

A biological catalyst that speeds up the rate of reaction by reducing the activation energy of reactions

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63
Q

What is the structure of an enzyme?

A

Globular protein with an active site and charged R groups on the outside of molecules (hydrophilic)

64
Q

Why are enzymes described as biological catalysts?

A

They are proteins which reduce the activation energy of biological reactions

65
Q

What is an active site

A

The active site is the region of catalytic function and it is complementary to the substrate
Highly specific due to their tertiary structure

66
Q

What is the effect of changing enzyme concentration on the initial rate of reaction?

A

Enzymes reduce activation energy. Active sites of enzymes become occupied but as substrate concentration decreases it becomes the limiting factor as not all active sites are occupied.

67
Q

What type of protein is an enzyme?

A

Globular, with complex tertiary structure

68
Q

What is the difference between intercellular and extracellular proteins?

A

Intercellular - produced and function inside cell

Extracellular - secreted by cells and catalyse reactions outside cells

69
Q

How do enzymes reduce activation energy?

A

By providing an alternative reaction pathway

70
Q

How can pH and temperature alter enzyme activity?

A

They can alter protein structure and change the shape of the active site - denaturation

71
Q

What must happen for a reaction to occur between the substrate and active site of an enzyme?

A

Substrates must collide with the active site at the correct orientation and speed in order for a reaction to occur

72
Q

What creates enzyme specificity?

A

The complementary nature of the active site and substrate

73
Q

What determines the shape of the active site of an enzyme, and what can alter this (apart from temp and pH)?

A

Determined by the complex tertiary structure of the protein
If the tertiary structure is altered in any way (different polypeptide chain sequence), the active site will change and the substrate will not fit

74
Q

What is the lock and key theory?

A

The theory that the substrate fits exactly into the active site

The substrate molecules form temporary binds with amino acids of the active site to produce an enzyme substrate complex

When the reaction has taken place the products are released, leaving the enzyme unchanged

75
Q

Why do enzymes only catalyse one specific reaction

A

Each enzyme will only catalyse one specific reaction because only one shape of substrate will fit into its precisely shaped active site

76
Q

What is the induced fit theory?

A

The enzyme and its active site (and sometimes substrate) can change shape slightly as the substrate molecule enters the enzyme

77
Q

How does the induced fit theory maximise the ability of the enzyme to catalyse a reaction?

A

Conformational change

Ensures an ideal binding arrangement between the enzyme and substrate

78
Q

what is activation energy

A

Conformational change

Ensures an ideal binding arrangement between the enzyme and substrate

79
Q

What is an active sites shape determined by

A

The active sites shape is determined by its tertiary structure which is determined by its primary structure

80
Q

What happens if an enzyme is altered to have a different tertiary structure

A

a different tertiary means a different shaped active site

If the substrate shape doesn’t match the active site, an enzyme substrate complex won’t be formed and the reaction wont catalyse - the enzyme will no longer be able to carry out its function

81
Q

What can change the active site

A

changes in pH or temperature
If a mutation occurs in that gene, it could change the tertiary structure of the enzyme produced

82
Q

how is the rate of reaction is measured

A

by determining the quantity of substrate used or the quantity of product formed in a given time
E.g. when the enzyme catalase is used to break down hydrogen peroxide to water and oxygen
The rate of reaction can be found by measuring the volume of oxygen given off in a known time

83
Q

What happens as substrates are used up

A

there are fewer substrate molecules to collide with and bind to the enzyme so reaction slows down and eventually stops and no further increase in the product occurs

enzyme concentration eventually has no further effect - substrate concentration has become a limited factor

84
Q

What does a steeper slope on an enzyme concentration graph mean

A

higher initial rate of reaction

85
Q

before substrate concentration becomes a limited factor, what happens in the reaction

A

The higher the substrate concentration, the faster the reaction - more substrate molecules means a collision between enzyme and substrate is more likely and so more active sites will be used

until a point of ‘saturation’

86
Q

what happens in a graph when all active sites are used

87
Q

What are nucleotides in DNA and RNA made from?

A

pentose sugar

nitrogen containing organic base

phosphate group

88
Q

What are the components of a DNA nucleotide?

A

Deoxyribose sugar with hydrogen at the 2’ position
Phosphate group
Organic bases A T C or G

89
Q

What are the components of an RNA nucleotide?

A

Ribose sugar with a hydroxyl (OH) group at the 2’ position
Phosphate group
Organic base A U C or G

90
Q

Which bases are purines, and what does this mean?

A

Purine = double ringed structure

A and G

91
Q

Which bases are pyrimidines, and what does this mean?

A

Pyrimidine = single ring structure

C, U and T

92
Q

What type of bonds join nucleotides in DNA and RNA?

A

Phosphodiester bonds

93
Q

How are phosphodiester bonds formed?

A

When separate nucleotides are joined by condensation reactions occurring between the phosphate group of one nucleotide and the pentose sugar of another. This creates a sugar-pentose backbone in DNA and RNA

94
Q

what are genes

A

a sequence of bases that codes for a sequence of amino acids

95
Q

structure of DNA

A

long chain polymer, it is a large molecule made up of many smaller units joined together
Each of these smaller units are nucleotides/mononucleotides
Every molecule of DNA is made of two strands
Each of the two strands is made from thousands of nucleotides
DNA molecules form a spiralling shape called a double helix

96
Q

whats a pentose sugar

A

a sugar with 5 carbons

97
Q

what are the names of the 4 possible DNA bases

A
  1. Adenine
  2. Thymine
  3. Cytosine
  4. Guanine
98
Q

Why is DNA antiparallel?

A

It is made up of 2 polynucleotides running in opposite directions

99
Q

How do the bases pair in DNA?

A

Purine A with pyrimidine T (2 H bonds)
Purine G with pyrimidine C (3 H bonds)
Hydrogen bonds form between complementary bases

100
Q

What is the difference between RNA and DNA?

A

RNA is only made up of 1 polynucleotide strand, whereas DNA is made up of 2
RNA = ribose sugar, DNA = deoxyribose sugar
RNA is relatively short compared to DNA

101
Q

What is the difference between transcription and translation?

A

Transcription occurs in the nucleus and is when DNA is transcribed and mRNA is produced

Translation occurs in the cytoplasm and is when mRNA is translated and a polypeptide is formed

102
Q

What happens in transcription?

A

Enzyme RNA polymerase unwinds DNA molecule, breaking H bonds, and exposing the gene to be transcribed.

RNA nucleotides line up and pair with complementary bases on the antisense/template strand.

RNA polymerase bonds the RNA nucelotides together to form the backbone of the mRNA molecule which then leaves via a nuclear pore and DNA reforms

103
Q

What is the difference between the antisense/template strand and the sense/coding strand?

A

The antisense/template strand is the strand used to make an mRNA copy

The other strand is known as the sense or coding strand as mRNA will have the same base sequence as this strand (T replaced by U)

104
Q

What direction does RNA polymerase move down the template strand, and why?

A

Moves in 3’ to 5’ direction as mRNA moves in 5’ to 3’ direction

105
Q

What happens in translation?

A

Once in cytoplasm, mRNA attaches to a ribosome. Each tRNA molecule has the complementary anticodon to the codon on the mRNA. tRNA molecules then form H bonds with the codons on the mRNA to bring amino acids, which form peptide bonds between amino acids. 2 tRNA molecules are on the ribosome at a time, the process continues until a stop codon, when the polypeptide chain moves away and translation is complete.

106
Q

What is translation

A

Turning the sequence of bases in the genetic code into a sequence of amino acids

107
Q

What is the role of tRNA in translation?

A

transport amino acids from cytoplasm to the ribosome
tRNA has an anticodon which binds to/recognises codon on mRNA
each tRNA carries a particular amino acid

108
Q

Why is a change in the sequence of bases of DNA an issue?

A

Could change a triplet that makes up a gene, which could then change the amino acid sequence of the primary structure which may substantially alter the proteins 3d shape and therefore properties

109
Q

What type of replication does DNA undergo, and what does this mean?

A

Semi-conservative, meaning that half of the strands in the new DNA molecule are from the original DNA molecule
This means there is genetic continuity between generations of cells

110
Q

How does the process of DNA replication occur?

A

Enzyme DNA helicase breaks hydrogen bonds between complementary bases. DNA strands unwind, and free floating nucleotides then align themselves with the correct base pairings. The enzyme DNA polymerase links the adjacent nucleotides with phosphodiester bonds in condensation reactions to form new complementary strands. DNA ligase used on lagging strand. This process is described as semi conservative because each new DNA molecule consists of one original (parental) DNA strand and one newly synthesised strand

111
Q

How did Meselsohn and Stahl’s experiment prove DNA replication was semi conservative?

A

Grew bacteria in cultures of a ‘heavy’ isotope of nitrogen (N15), and after many generations bacteria was transferred to a medium with a lighter isotope of nitrogen (N14). DNA was extracted from bacteria after 1, 2 and several rounds of replication and centrifuged after each replication.
1st replication - single band of ‘medium’ density produced ruling out conservative replication (could be dispersive or semi conservative)
2nd replication - formed 2 bands, one half heavier than other (one uses N15 as template and other N14)

112
Q

How do we know that DNA replication is semi-conservative?

A

Meselsohn and Stahl experiment

Used heavy and light strands of DNA to distinguish method of DNA replication

113
Q

What were the different modes of DNA replication suggested before Meselsohn and Stahl’s experiment?

A

Conservative - strands separate but new strands join together to form entirely new molecule and ‘old’ strands stay together
Semi-conservative - strands separate and are joined by a new strand
Dispersive - new DNA mixture of both old and new DNA

114
Q

Which direction can DNA polymerase build the new strand in?

A

ONLY in the 5’ to 3’ direction

115
Q

What strand is the leading strand, and what does this mean?

A

The original DNA strand starting at 3’, meaning it can be synthesised by DNA polymerase continuously, moving towards the replication fork

116
Q

What strand is the lagging strand, and what does this mean?

A

The other DNA strand where DNA polymerase moves AWAY from the replication fork from the 5’ end. This means DNA polymerase can only synthesise the strand in short segments called Okazaki fragments, and DNA ligase is required to join the lagging strand segments

117
Q

What is the role of DNA ligase and how does it work?

A

To connect lagging strand segments

It catalyses the formation of phosphodiester bonds to form a continuous strand

118
Q

What is cystic fibrosis?

A

A recessive genetic disorder of the cell membrane, where abnormally thick and stick muscus is produced in the body’s passageways

119
Q

What causes cystic fibrosis?

A

A mutation in the CFTR gene which leads to production of non functional chloride ion channel proteins, reducing the movement of water via osmosis into the mucus

120
Q

What impacts does cystic fibrosis have on the respiratory system

A

-cilia unable to move thick and sticky mucus so microorganisms are not removed from the lungs and -lung infections occur more frequently
-mucus builds up in the lungs and can block airways, limiting gas exchange
-SA for gas exchange reduced, causing respiratory issues

121
Q

What impacts does cystic fibrosis have on the digestive system?

A

can block pancreatic duct, preventing digestive enzymes from entering the small intestine, meaning key nutrients may not be available for absorption

122
Q

What impacts does cystic fibrosis have on the reproductive system?

A

mucus can cause fertility issues
in men: tubes of testes blocked, preventing sperm reaching penis
in women: thickened cervical mucus can prevent sperm reaching the oviduct to fertilise an egg

123
Q

What are the differences between somatic gene therapy and germ line gene therapy?

A

Somatic = body cells, germ line = all cells, including gametes
Somatic is legal, germ line illegal
Somatic therapy is temporary treatment, germ line can be inherited

124
Q

How can somatic gene therapy enable cells lining the lungs to function normally in people with CF?

A

Functional gene that codes for CFTR inserted into a plasmid, which is then put into the lungs via a nebuliser. The CFTR protein is made (transcription/translation) allowing chloride ions to leave the cells, and water follows via osmosis. This reduces the stickiness of the mucus.

125
Q

How can rhythmical tapping of the chest wall during physiotherapy relieve the symptoms of CF in the lungs?

A

Loosens mucus, expelled from lungs more easily, clearer airways and better breathing

126
Q

Why do people with CF have breathing difficulties?v

A

Mucus is more viscous and sticky - this means it builds up and blocks trachea/bronchioles and the cilia are unable to remove it.

Reduced air flow to alveoli, reduced concentration gradient for gas exchange, loss of surface area and elasticity = reduced gaseous exchange

127
Q

What types of genetic mutation are there?

A

deletion
insertion
substitution
inversion
duplication

128
Q

How can a gene mutation affect protein structure?

A

A change in base sequence causes a change in amino acid/primary structure of a protein. This causes different R groups to be formed, leading to different types of bonding, which can alter the shape of the protein.

129
Q

What is an insertion mutation and how does it affect transcription and translation?

A

When a nucleotide is randomly inserted into the genetic code
Can cause a frame shift by altering triplets downstream, potentially dramatically changing the amino acid sequence and therefore polypeptide function

130
Q

What is a deletion mutation and how does it affect transcription and translation?

A

Where a nucleotide is randomly deleted

Causes a frame shift and changes every subsequent triplet, can affect amino acids sequence and also polypeptide function

131
Q

What is a substitution mutation and how does it affect transcription and translation? (different types?)

A

Where a base in DNA is randomly swapped for another - this will not have knock on impacts
Silent - no change due to degenerate nature of genetic code
Missense - single amino acid changed
Nonsense - premature stop codon

132
Q

What is a duplication mutation and how does it affect transcription and translation?

A

Production of one or more copies of a gene/region of a chromosome. 2 copies of the gene appear on the same chromosome.
Mutation not harmful

133
Q

What is an inversion mutation and how does it affect transcription and translation?

A

During the crossing over of meiosis, DNA of a single gene is cut but inverted 180 degrees before being rejoined to the same region.
This frequently results in a non functional protein as the original gene can no longer be expressed

134
Q

Why does a substitution mutation have less effect than a deletion mutation?

A

Deletion mutation causes frame shift and whole amino acid sequence to change.
Substitution mutation only changes one codon/amino acid, number of amino acids remains the same

135
Q

What is a gene?

A

sequence of bases/nucleotides in DNA
that codes for the primary structure/amino acid sequence/polypeptide

136
Q

What are alleles?

A

Alternative forms of a gene occupying the same locus on a chromosome

137
Q

What is genotype?

A

All of the alleles an organism carries on it’s chromosomes

138
Q

What is phenotype?

A

The observable characteristics of an organism

139
Q

What do homozygous and hetereozygous mean?

A

Homozygous - Pair of alleles that produce a characteristic that are the same, e.g. HH or hh
Hetereozygous - Pair of alleles that will produce a characteristic that will be different e.g. Hh

140
Q

What is the difference between a dominant and recessive allele?

A

Dominant - always expressed

Recessive - only expressed if no dominant allele is present

141
Q

What is the meaning of the term recessive allele?

A

Both alleles must be present in order for recessive phenotype to be expressed.
AND different form of a gene/same locus/different base sequence

142
Q

What is incomplete dominance?

A

Where a trait from a dominant allele is not completely expressed over the recessive allele trait (it ‘dilutes’ it)

143
Q

What is monohybrid inheritance?

A

The inheritance of a characteristic controlled by a single gene

144
Q

Who is Mendel and what did he do for genetics?

A

He was a monk and carried out a huge number of breeding experiments between garden pea plants. He established ‘heredity units’, which are now called genes

145
Q

What is the use of pedigree diagrams?

A

Family pedigree diagrams can be used to trace the pattern of inheritance of a specific trait, e.g. a genetic disorder, through generations of a family

146
Q

What are the types of genetic screening?

A

identification of carriers

preimplantation genetic diagnosis

pre natal testing

147
Q

How does PIGD work and what are the benefits and issues?

A

PIGD = pre implantation genetic diagnosis
Analysis of genes in embryos created through IVF to check for genetic conditions
BENEFITS: reduces chance of having baby with genetic disorder, avoids abortion
ISSUES: ‘designer babies’, false results lead to poor decisions

148
Q

What is amniocentesis?

A

A diagnostic test carried out during pregnancy, performed at 14-20 weeks and involves inserting a needle into amniotic fluid to collect cells that have fallen off the placenta and foetus

149
Q

What is CVS and how does it work?

A

CVS = chronic villus sampling
A test carried out during pregnancy where a sample of cells are removed and tested from the placenta. Checks baby for inherited disorders such as Down’s syndrome and rarer diseases

150
Q

What are the benefits and issues with pre natal testing?

A

BENEFITS: allows parents to make informed decisions, can help parents prepare for future of the child
ISSUES: each procedure brings risk of miscarriage, ethical implications if choice made for abortion

151
Q

What is the identification of carriers and what are the benefits and issues with it?

A

Genetic testing carried out on adults to show whether people with no symptoms carry the allele for particular disorders
BENEFITS: families can make informed decisions before choosing to become pregnant, women can decide to have prenatal testing
ISSUES: finding out you’re a carrier can cause emotional stress, hard to find a partner, employers and insurance may use information against you

152
Q

What are some of the ethical and social issues related to genetic screening?

A

Embryo has a right to life (abortion is murder)
False positives or negatives
Who has right to decide if tests should be performed
Risk of miscarriage of healthy child
More stress for parents.

153
Q

Advantage and disadvantage to parents genetic screening their fetus?

A

Adv - allows them to make an informed choice, prevents baby dying in pregnancy
Disadv - cause parents emotional stress, risk of false positives/negatives, can cause miscarriage of healthy child

154
Q

Why do cigarette smokers have a higher risk of developing lung cancer than non smokers?

A

Cigarettes contain carcinogens/are an environmental risk factor
This increases the number of mutations in cells, increasing the risk of uncontrolled cell division.

155
Q

What is an inherited recessive disorder?

A

Caused by a faulty allele
Only expressed in homozygous condition