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AS Biology > Genes And Health > Flashcards

Genes And Health Flashcards

1
Q

What is the function of mucus?

A
  • Traps foreign particles (dust, bacteria) and prevents them from entering the airways
  • moisturises inhaled air (to aid diffusion)
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2
Q

What are the properties of gas exchange surfaces in living organisms?

A
  • large sa/v ratio
  • thin surface - short diffusion distance
  • high concentration gradient
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3
Q

Ficks law - calculating rate of diffusion

A

The rate of diffusion is inversely proportional to the thickness of the gas exchange surface

rate of diffusion directly proportional to
SA x difference in conc
——————————
diffusion distance

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4
Q

How CF affects the respiratory system?

A

(breathing difficulties due to reduced gas exchange)

  • less air can be breathed out - over inflation of the lungs causes elasticity of lungs decreases
  • mucus blocks bronchioles: fewer alveoli available for gas exchange
  • mucus fills alveolus: longer diffusion distance
  • (Harder to breathe, exercise)
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5
Q

Gas exchange on outer surface of a land-living (terrestrial) organism?

A
  • Outer surface for protection, not gas exchange
  • high water content in mammal compared to the surrounding air, so would dry out
  • outer layer is very thick, long diffusion distance ensures slow gas exchange
  • have internet gas exchange surfaces to reduce evaporation losses
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6
Q

Multicellular aerobic respiration why?

A

Because they require a lot of energy and aerobic produces 19 times more ATP (adenosine triphosphate) per molecule of glucose

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7
Q

Gas exchange in other organisms:

A

Unicellular organisms: build up of CO2 - high conc gradient and thin surface membrane

Insects: hard exoskeleton unsuitable for gas exchange, lack of transport system - gas exchange through outer surface (short diff distance)
& tracheoles - large SA and they also contain fluid so glasses diffuse efficiently

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8
Q

How are alveoli adapted for efficient gas exchange?

A
  • both endothelium and epithelium are 1 cell thick so short diffusion distance
  • constant flow of blood and air flow from breathing so steep concentration gradient is maintained
  • folded shape of alveoli, many alveoli and capillaries - large SA/v ratio
  • pulmonary surfactant prevents the alveoli from collapsing
  • moisture dissolves gases to allow diffusion + prevents lung tissue drying out
  • close to capillaries - short distance
  • smoking: destroys alveolar walls, decreased SA for gas exchange, decreased diffusion rate
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9
Q

Primary structure of proteins:

A

= The linear sequence of the amino acids in a protein

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10
Q

Secondary structure of proteins:

A

= Regular 3D structure formed due to hydrogen bonds between the H and O of PEPTIDE BONDS

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11
Q

Secondary structure - Alpha Helices

A

polypeptide chain wound round to form helix (many H bonds so have very strong, stable structure) - held together by hydrogen bonds running parallel with the long helical axis

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12
Q

Secondary structure - Beta pleated sheet

A

Polypeptide chain zig zags back and forward forming a sheet of anti parallel strands

Held together by H bonds between peptide bonds

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13
Q

Tertiary structure of proteins:

A

= 3D structure of the whole peptide chain, formed by hydrophobic interactions,
hydrogen bonds,
ionic bonds,
disulphide bonds between R GROUPS

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14
Q

Bonds involved in making up tertiary structure from weakest to strongest:

A

hydrophobic interactions between R groups

hydrogen bonds (between H and O)

ionic bonds between charged R groups

disulphide (covalent) bonds between cysteine R groups

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15
Q

Quaternary structure of proteins:

A

= The 3D structure of several polypeptide chains joined together

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16
Q

Conjugated proteins:

A

= proteins that are joined to other non-protein molecules (known as prosthetic groups e.g the Haem in Haemoglobin)

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17
Q

Globular proteins:

A

Proteins with a complex tertiary (sometimes quaternary) structure

  • folded into spherical shapes (hydrophobic parts on the inside)
  • soluble (hydrophilic parts on the outside)

• often small

E.g enzymes, antibodies, hormones
-insulin (51 aa)

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18
Q

Fibrous proteins:

A

= proteins that have little/no tertiary structure

  • form long fibres made of several polypeptide chains
  • insoluble
  • often large
  • strong

-structural role (e.g tendons)
-collagen (>1000 aa)
& Collagen has repeating sequences of amino acids

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19
Q

Why may the increase in temperature increase the length of the secondary structure of the polypeptide?

A

Increase in kinetic energy, more vibrations within the molecule that could break the hydrogen bonds - molecule unwinds

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20
Q

What surrounds the goblet cells and what are they attached to?

A

Ciliated columnar epithelial cells - attached to basal membrane that holds them in place

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21
Q

What is the fluid mosaic model?

A

1972 Singer and Nicholson’s membrane model:
Proteins are through the membrane, not holding phospholipids in place

• by increasing ionic strength of solutions or by adding protease-containing detergents, some proteins can be removed from membrane

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22
Q

What are the components of a phospholipid?

A

Hydrophilic phosphate heads face towards the solution (& polar)

Hydrophobic fatty acid tails face away from the solution (& non-polar)

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23
Q

What’s glycocalyx?

A

Protective role on membrane (carb part of glycolipid)

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24
Q

Why is it called the fluid mosaic model?

A

Fluid - because of the lateral movement of lipids and proteins through the bilateral

Mosaic - composed of many different macromolecules

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25
Q

What are other components of membranes?

A

Peripheral protein (cellular communication - on the surface), cholesterol, integral protein (on inside layer), integral transmembrane protein - channel proteins (across whole bilayer)

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26
Q

Increase membrane fluidity:

A

More unsaturated (double bonds, bends in chains) fatty acids, phospholipids less tightly packed (more movement possible)

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27
Q

Decreasing membrane fluidity:

A

more cholesterol, less fluid- prevents movement of phospholipids

(But if there is too little cholesterol, it is too fluid- disrupts structure)

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28
Q

What affects the degree of fluidity of cell surface membranes?

A

The length of the fatty acid side chains (longer - less fluid)

The proportion of the fatty acids which are saturated (higher percentage of saturated - lower fluidity)

The steroid (cholesterol) content (higher steroid content - lower fluidity)

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29
Q

PASSIVE transport definitions:

A

Diffusion: the movement of molecules from an area of high to low concentration

Facilitated diffusion: the movement of molecules from an area of high to low concentration via a carrier protein (across a membrane)

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30
Q

Osmosis definition:

A

The movement of water molecules from high to low water potential across a partially permeable membrane

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31
Q

Active transport:

A

= movement from low to high concentration via carrier proteins and using energy from ATP

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32
Q

Endocytosis:

A

= uptake of molecules starting with invagination of the cell membrane and resulting in the formation of vesicles (bulk transport into cell)

‼️ requires energy

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33
Q

Exocytosis:

A

= when vesicles fuse with the cell memes be and release their contents (bulk transport out of the cell)

‼️ requires energy

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34
Q

Hypotonic solution:

A

= lower solute concentration than inside cell

(When a plant/animal cell is in this kind of bathing solution, water moves into the cell by osmosis, leaving the cell lysed (in an animal cell) or turgid (in a plant cell ‼️ this is normal for a plant)

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35
Q

Isotonic solution:

A

= same solute concentration as inside cell

no net movement of water (plant flaccid, normal for an animal)

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36
Q

Hypertonic solution:

A

= higher solute concentration than inside cell

(When a plant/animal cell is in this kind of bathing solution, water moves out of cell/vacuole by osmosis, leaving the cell shrivelled (in an animal cell) or plasmolysed (in a plant cell)

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37
Q

Channel and carrier proteins:

A

Channel proteins are for polar molecules eg ions

Carrier proteins are for larger molecules eg glucose

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38
Q

Mucus formation in healthy people (with excess water)

A

Na+ actively pumped across basal membrane

Na+ diffuse through sodium channels in the apical membrane

Cl- diffuses down electrical gradient

Water moves out of cells by osmosis due to high salt conc into the tissue fluid

Water moves out of mucus by osmosis

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39
Q

Mucus formation in healthy people (with too little water)

A

Cl- actively pumped into cell from tissue fluid across basal membrane

CFTR channel is open and causes Na+ channel to close. Cl- diffuses through the open CFTR channel

Na+ diffuses down electric gradient into the mucus

Elevated salt conc in mucus draws water out of the cell by osmosis. Water diffuses into mucus + makes it more running

Water is drawn into cell from tissue fluid by osmosis

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40
Q

Enzymes:

A

Globular proteins that act as biological catalysts and reduce activation energy

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41
Q

Enzymes that catalyse reactions inside cells:

A

Intracellular enzymes

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42
Q

Enzymes that catalyse reactions outside cells:

A

Extracellular enzymes

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43
Q

Cofactors:

A

= non-protein chemical compounds that are bound to enzymes + required for enzyme action

coenzymes - loosely bound cofactors (vitamin c + metal ions)

prosthetic group - tightly bound cofactors (eg heme group)

44
Q

Competitive inhibitor:

A

= compete with substrate for active site

45
Q

non- competitive inhibitor

A

= bind to allosteric site + influence shape of active site

46
Q

turnover number:

A

= number of substrate molecules transformed by one molecule of enzyme per second

47
Q

Substrate and enzyme concentration as an affect on rate of reaction of an enzyme:

A

For either:
1) lower concentration, not all active sites occupied/few ES complexes formed, slow rate of reactive

2) high concentration - (/more active sites➡️) more ES complexes, higher rate
3) IF more substrate than enzyme, all active sites occupied, increasing substrate has so affect - max rate of reaction (V max) ➡️ depends on turnover number of enzyme
3) more enzyme than substrate, increasing enzyme conc has no more affect, substrate has become limiting factor

48
Q

Active site:

A

Part of the folded protein where the substrate(s) bind

When all the active sites are occupied - enzyme is saturated

49
Q

why measure the initial rate of reaction?

A

As reaction goes on, there is a decreasing about of substrate but the concentration of enzyme stays the same. This lessons the chances of a collision between a substrate molecule and an enzyme.
➡️ at the initial rate, most valid measurement, when rate of reaction is under the desired conditions, (much higher amounts of substrate than product)

50
Q

How can CF cause lung infections?

A
  • thick, dry mucus lines airways and traps bacteria but too sticky to be moved by cilia ➡️ inflammation + infection
  • low o2 levels in mucus: anaerobic bacteria thrive
  • WBC fighting bacteria die + release DNA making mucus stickier
51
Q

How does CF impair the functioning of the digestive system?

A

Thick sticky mucus in the pancreatic duct + small intestine

➡️impaired digestion

  • digestive enzymes made in pancreas can’t reach small intestine
  • reduced digestion of food
  • reduced nutrients uptake (longer diffusion pathway + reduced SA)

➡️ damage to pancreas

  • trapped enzymes damage pancreas
  • islets of langerhans might be damaged + insulin production affected
52
Q

How does CF impair the functioning of the reproductive system?

A
  • infertility
  • thick sticky mucus in the reproductive system

FEMALE - TSM blocks cervix and oviducts
-sperm cannot get past mucus plug

MALE - sperm duct might be missing/blocked by TSM

  • reduced number of sperm can leave testes (reduced sperm count)
  • reduced fertility
53
Q

How does CF affect sweat production?

A

• in healthy people, (sweat = salty water made in sweat glands) salt is reabsorbed out of sweat duct into cells (Cl- via CFTR, Na+ follow by diffusion)

• but in CF sufferers, in the absence of functional CFTR, Cl- and Na+ are not reabsorbed + instead are lost in sweat
- conc of body fluids changes (may affect the heart)

54
Q

Why may an enzyme have a low pH optimum? (Acidic)

A

Eg pepsin catalysed reactions in the stomach in acidic conditions

55
Q

What is the structure of a mononucleotide?

A

Deoxyribose/ribose (pentagon as pentose sugars) linked to a phosphate (circle) and a base

56
Q

What are the general structures of DNA/RNA?

A

polynucleotides composed of mononucleotides linked through condensation reactions

57
Q

Which bases have a single ring structure?

A

Thymine/Uracil and Cytosine

PYRIMIDINES

58
Q

Which bases have a double ring structure?

A

Adenine and Guanine

PURINES

59
Q

What are the steps of nucleotide formation?

A

Sugar joins base in condensation reaction = nucleoside (base + sugar)

phosphate joins sugar side of nucleoside in condensation reaction = nucleotide

60
Q

What is a phosphodiester bond?

A

The bond between the OH and H from one sugar and the adjacent phosphate when they form the backbone of DNA in a condensation reaction.

61
Q

Which bases form 3 or 2 hydrogen bonds?

A

A … T with 2 hydrogen bonds

G … C with 3 hydrogen bonds

62
Q

Differences between DNA and RNA?

A

the sugar they contain

the bases

the structure - RNA is single stranded

the length - RNA is made of shorter strands and DNA is very long

the location - DNA is always in the nucleus, RNA is made in nucleus but found throughout the cell

the amount - DNA amount constant in cells, RNA varies from cell to cell

stability - DNA is chemically very stable, RNA is chemically unstable

63
Q

Define the genetic code:

A

The DNA code that ensures amino acids are arranged in the correct sequence in proteins

64
Q

What is the nature of the genetic code:

A

Triplet code: 3 bases (a codon) codes for 1 amino acid

It’s degenerate: one amino acid can be coded for by more than one codon

Non-overlapping (each codon is read separately)

ALSO ➡️
Universal: same code in all organisms

TAA, TAG, TGA (the 3 stop codons) don’t code for an amino acid

65
Q

Define transcription and where does it occur?

A

The copying of DNA into messenger RNA (mRNA)

-it occurs in the nucleus

66
Q

What catalyses transcription?

A

RNA polymerase

67
Q

What are the steps in transcription?

A
  1. RNA polymerase binds to promoter region
  2. RNA polymerase unwinds double helix and starts to transcribe DNA sequence on the anti-sense (template) strand into RNA sequence through complementary base pairing. ➡️ free nucleotides line up by complementary base pairing
  3. RNA transcript is made (and is same as coding strand with U instead of T)
  4. after RNA polymerase reaches termination point, transcription stops and RNA polymerase detaches
  5. RNA sequence is spliced (introns are removed) and processed
  6. RNA is translocated out of nucleus via pores in the nuclear envelope
68
Q

Define translation and where does it occur?

A

Translating mRNA sequence into an amino acid sequence

Occurs on ribosomes in the cytoplasm or on the rough endoplasmic reticulum

69
Q

What are the steps in translation?

A
  1. Amino acid binds to corresponding tRNA
  2. mRNA attaches to ribosome and ribosome moves along to the AUG (start codon). ribosome loads tRNA with complementary anticodon UAC.
  3. Ribosome moves a long and loads the next tRNA. adjacent amino acids join via a peptide bond (catalysed by peptide synthetase). when it loads the third tRNA, it releases the first one
  4. ribosome reaches stop codon and release factor stops translation. ribosome separates- polypeptide chain complete
70
Q

What is a polysome?

A

mRNA with several ribosomes attached. several ribosomes can bind to the same mRNA so that several polypeptide chains are synthesised at the same time

71
Q

what is the structure of tRNA

A

Is folded with a tertiary structure and has hydrogen bonds.

Has anticodons (at bottom)
Has an amino acid binding site (at the top)
72
Q

What structure is mRNA?

A

primary structure

73
Q

What are the steps of DNA replication?

A
  1. DNA helicase unwinds the DNA double helix
  2. two strands are separated as H bonds break
  3. Each parent strand is a template for a new DNA strand. DNA polymerase pairs new nucleotides with complementary nucleotides (nucleotides join together forming phosphodiester bonds)
  4. two identical new DNA strands are exposures and they rewind into a helix
74
Q

Why is replication considered ‘semi-conservative’

A

Each new DNA molecule has one strand of original parent DNA and one new strand

75
Q

What were the theories about DNA replication and who proved the right one?

A

Semi-conservative
dispersive - 2 DNA molecules made randomly of 50% new and 50% old DNA
conservative - one molecule completely old and one completely new

Meselson and Stahl’s experiment

76
Q

How can errors in DNA replication lead to mutations?

A

Eukaryotic DNA polymerase makes 1 mistake in every 10-100k base pairs but it has ‘proof reading’ enzymes to correct mistakes

So ~1 mistake in every 10 mil base pairs per cell division

mutagens can lead to chemical changes in bases, errors during replication

77
Q

What are the types of gene mutations?

A

Point mutation - change in a single base(nucleotide)

Frame shift mutation - the reading frame changes and results in a different protein sequence (insertion/deletion of a nucleotide)

Substitution - a nucleotide is replaced by another base

Inversion - two nucleotides are swapped

78
Q

What are the names given to the affect in the sequence of types of mutations?

A

Silent mutation - no change in amino acid sequence (bc it’s a degenerate code)

Missense mutation - change in the amino acid sequence

Nonsense - premature stop codon ➡️ non functional protein

79
Q

How can a mutation be inherited?

A

Somatic mutation- mutation not passed on

Germ line mutation - in germ cell, passed on ➡️ mutation would be in every body cell and 50% chance of them in sex cells (because 1 of each chromosome)

80
Q

How can a genetic disease suddenly appear in a family with no previous history of the disease?

A

By a random mutation in the genes causing a faulty protein to be produced.

81
Q

Relief of symptoms of CF for respiratory system?

A

medications to relax muscles in airways (bronchodilators)

antibiotics to fight infections

DNAase enzymes to break down DNA from WBCs

steroids to reduce inflammation in lungs

Or phsyio therapy to dislodge mucus from lungs

heart/lung transplant

82
Q

Relief of symptoms of CF for reproductive system?

A

Fertility treatment: IVF

83
Q

Relief of symptoms of CF for digestive system?

A

diet: high energy food, high protein, salt supplements

digestive enzymes supplements - to help digestion

84
Q

Define gene therapy:

A

= inserting a new gene into the cell nucleus to replace a defective gene that causes a disorder

85
Q

What vectors can you use for gene insertion in gene therapy?

A

Liposomes (eg spherical cationic phospholipid bilayers)

Viruses (eg retroviruses)

86
Q

What are the steps involved in gene therapy using liposomes?

A

1) CFTR gene is inserted into plasmid using restriction enzyme and DNA ligase ➡️ recombinant DNA
2) plasmids are mixed with liposomes - the negatively charged DNA is attracted to positively charged head groups of phospholipids
3) liposome-DNA complex forms and fuses with cell membrane ➡️ DNA is brought into cell and moves into nucleus

(( 4) CFTR gene is transcribed, mRNA moves to RER and it is transcripted. Functional CFTR is produced and targeted to plasma membrane ))

87
Q

What are the pros of gene therapy using liposomes?

A

Liposome-DNA complexes can be breathed in as an aerosol using a nebuliser (easier to administer)

Up to 25% restoration of CFTR function in lung epithelial cells - alleviation of symptoms

88
Q

What are the cons of gene therapy using liposomes?

A

DNA not inserted into target cell DNA, effect does not last as the DNA isn’t replicated

Not all cells receive the liposome-DNA complex (due to TSM) ?

89
Q

What are the pros of gene therapy using viruses?

A

Virus can be breathed in as an aerosol using a nebuliser (easy to administer)

DNA inserted into cells own DNA and thus replicated as cells divide (only some type of viruses this way)

➡️ more effective way to get CFTR gene into cells

90
Q

What are the cons of gene therapy using viruses?

A
  • inflammatory response (side effects of virus: headache, fever)
  • insertion of DNA into cells’ DNA may destroy other genes
91
Q

What are the steps of gene therapy using viruses?

A

1) take out DNA sequence that allows virus to replicate and insert CFTR gene (with promoter and other regulatory DNA sequences)
2) cells are infected with the virus; viral DNA with CFTR gene is incorporated into the cells DNA (or remains independent in the cell if other type of virus is used)
3) CFTR gene is transcribed and translated and functional CFTR protein is produced

92
Q

What is somatic gene therapy?

A

= Gene therapy of normal body cells

Not all cells receive the healthy allele

Mutation still passed on to next generation

93
Q

What is germ line therapy?

A

= gene therapy of cells that produce gametes (gametocytes)

During embryo development, the healthy allele is inserted- gametocytyes receive healthy allele so that gametes are healthy and mutation is not passed on

Potential abuse - people would use it to change skin colour, adult height (illegal in the U.K.), potential defects in embryo, offspring have no say in whether or not their genetic material is modified

94
Q

Ethical for gene therapy?

A

Reduced suffering
Increase qualify and length of sufferers life

In theory could get rid of some genetic diseases

Can be used where conventional treatment has failed

The right to research of scientific community (doesn’t mean they have to use)

95
Q

Ethical against gene therapy?

A

Slippery slope - changing traits about themselves such as skin colour

too much scientific uncertainty- Not sure yet of long term effects, could be apparent later

germ line - lack of consent of embryo, and violating rights of future generations

96
Q

What is carrier testing?

A

Take samples of cheek cells and test DNA to see if it contains most common mutations in CFTR gene

(80-85% reliable sometimes false negatives with unknown mutations)

97
Q

Explain IVF (and PGD)

A

Remove eggs from ovaries and fertilise with sperm in a test tube

A cell is removed from the resulting embryos at the 8-16 cell stage and their DNA is tested for mutations associated with CF

Choose embryo which does not carry faulty alleles

98
Q

What is PGD?

A

Preimplantation genetic diagnostic

99
Q

What is prenatal screening and the two different types?

A

To check if the foetus has CF:

Amniocentesis
chorionic villus sampling (CVS)

100
Q

What is involved in cvs?

A

Chorionic villus sampling:

During 8-12 weeks pregnancy - sample of placental tissue, including cells of foetus, is removed through wall of abdomen or vagina

DNA is analysed

101
Q

What is involved in amniocentesis?

A

During 14-16 weeks pregnancy - a needle is inserted into the amniotic fluid and cells that have fallen off the placenta and foetus are collected

DNA is analysed

102
Q

Amniocentesis vs CVS

A

Amniocentesis is carried out later in pregnancy, CVS is earlier (better to have an early abortion?)

2-3 weeks to get results of amniocentesis, CVS results available next day

0.5-1% chance of miscarriage with amniocentesis, 1-2% in CVS

103
Q

What is involved in newborn screening?

A

Heel prick test - blood sample 5-14 days after birth and DNA is analysed

104
Q

What is an ethical framework?

A

= ethical guidelines that can be applied in order to make an ethical decision

105
Q

What are the ethical frameworks it genetic screening?

A

Rights and duties - baby right to life/ parents duty of care/ parents right to comfortable life without strain

Utilitarianism (maximising amount of good in the world) - is it good to bring a suffering child into the world?/ is a suffering child not worthy of being born?/ abortions?

Autonomy - make decision for yourself/ conflict with father?/ selfish?/ what about the affect on the foetus?

Virtues - eg faith and hope ➡️ no faith/hope that the baby will have a good life; justice - not having the abortion/having the abortion

AS Biology (4 decks)

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