AS BIOLOGY

UNIT 1

Keywords
Genotype - combination of alleles

Chapter 1A
-chemistry of life

Ionic bonding
● When ionic substances dissolve in water - called dissociation
● Most of our body is water so most compounds exist as positive and negative ions
● Play a specialized roles in cells
● Nitrates - used in making amino acids and proteins
● Phosphates - making of dna,rna,adp,atp
● Chloride- used in the sweating and secretory system and nerve impulses
● HCO3- used as a pH buffer
● Calcium - used for the formation of calcium pectate for middle lamella between 2 cell walls in plants and
bone formation and muscle contraction
● Sodium- used in the sweating,nerve impulses and secretory system
● Hydrogen - used in cellular respiration, photosynthesis and pH balance
● Magnesium - used for making chlorophyll

Covalent bonding
● Makes strong bonds
● They have neutral molecules
● Some covalent compounds have slightly polarized molecules - the electrons in the covalent bonds are
not evenly shared
● The molecule will have a negative and positive part
● The separation of charge is called dipole
● Results in tiny charges represented as S+ and S-
● The molecule is described as a polar molecule
● Polarity is common if the bond involves 1 or more hydrogen atoms

Water
● Is a polar molecule since the electrons are held closer to the oxygen
● Due to the polarity water molecules form hydrogen bonds- each individual H bond is weak but there are
many so the molecules of water “stick together”
● High MP and high BP
● Is a polar solvent so ionic and covalent substances both dissolve in it
● Is a good transport medium because the dipole nature of water allows different substances to dissolve
 ● Ice is less dense than water and floats , providing an insulating layer and preventing water beneath it
from freezing
● Has a specific heat capacity so temperatures of large water bodies don't change much throughout the
year
● Cannot be compressed - imp factor in the hydraulic mechanisms in the body
● Cohesive molecules - allows for the movement of water from root to leaf
● Adhesive features
● Has surface tension - attraction between water molecules greater than attraction between it and air so
the molecules hold together forming a thin skin of surface tension

Carbohydrates - a usable energy source and imp for energy storage

Monosaccharides
● Simple sugars
● CH2O formula
● Triose - important in mitochondria where the glucose broken into triose
● Pentose - found in dna - deoxyribose and in rna - ribose
● Hexose - tastes sweet and includes glucose , galactose and fructose
● Glucose has 2 isomers - alpha-z and beta -e glucose. The difference is the diff arrangement of
the atoms on the side chains of the molecule - refer page 9 for diagram

Disaccharides

● 2 monosaccharides joined together in a condensation reaction by releasing a water molecule

● Bond between 2 monos is called GLYCOSIDIC BOND
● Sucrose - made of glucose and fructose - stored in plants
● Lactose - made of glucose and galactose - main carb in milk
● Maltose -made of glucose and glucose - malt sugar found in germinating seeds

Energy is supplied by a substance called ATP - adenosine triphosphate and comes from breakdown of glucose

Other monosaccharides and disaccharides can be absorbed in the body from food and are a good source of
instant energy . They are converted to glucose but they are very reactive and soluble in water and affect water
balance therefore cannot be used to store the energy.

Polysaccharides
● Complex carbohydrates
● Made of many monosaccharide units joined by condensation reactions that create a glycosidic bond.
Can be broken down to release monosaccharides for respiration
● Molecules between 3-10 sugar units - oligosaccharides
● Molecules between 11 and more - true polysaccharides
● Hydrolysis is used to break it down - it happens during digestion in the gut as well as in muscle and liver
cells where carb stores are broken down to release sugars for cellular respiration
● Ideal energy storage molecule in a cell
● Is Compact
● Physically , chemically inactive - don't interfere with functions of a cell
● Not very soluble in water

Starch
● Insoluble , compact , broken down easily to release glucose
● Consists of long chains of alpha glucose
 ● Mixture of two compounds - combination of straight chain amylose and branched chain amylopectin
● Amylose - unbranched polymer of between 200-5000 glucose units. As the chain lengthens ,
becomes more spiral , more compact - 1,4-glycosidic bonds only
● Amylopectin - branched polymer of glucose units and branching chains have many terminal
glucose units that can be broken off rapidly when glucose is needed - 1,4 and 1,6-glycosidic
bonds resulting in the branching chain

Glycogen
● Similar to amylopectin in starch
● Many alpha glucose units
● 1,4 bonds and many 1,6-glycosidic bonds, more than amylopectin
● Many side branches
● Broken down rapidly

Carbs

Monosacchari Polysaccharid
Disaccharide
des es
Triose s
Sucrose Starch
Pentose
Lactose Glycogen
Hexose
Maltose
Glucose,galactose,fruc
tose

Lipids

● Used as an energy store

● Contains carbon,hydrogen but little oxygen
● Store 3 times as much energy as the same mass of carbohydrates
● Fats and oils are important groups of lipids - Fats are solid from animals while oils are liquid from plants
 ● Fats and oils contain 2 types of organic substances - fatty acids and glycerol which are combined using
ester bonds
● All fatty acids have long hydrocarbon chains - a folded backbone of carbon atoms with hydrogen
atoms attached and a COOH carboxyl group at one end
● Differ based on carbon chain length and if they are saturated or not
● Saturated with a single bond - stearic acid
● One c=c double bond - Monounsaturated
● More than one c=c double bond - polyunsaturated - linoleic acid
● Triglyceride - glycerol combines with 3 fatty acids
● Bond formed between carboxyl group of fatty acid and hydroxyl group of glycerol and is an ester
bond C=O-O

LIPIDS

fats oils

Fatty acids glycerol

Linoleic
Stereic

triglyceride

Proteins

● Contain C,H,O,N and some have sulfur

● Make hair, nails , skin , enzymes and hormones , antibodies, haemoglobin (allow O2 transport) , help in
blood clotting and protect from diseases
● Macromolecules made up of many small monomer units called amino acids joined by condensation
reaction

● Amino acids have an amino group NH2 and a carboxyl group COOH
 ● R group varies between amino acids
● Not involved in reactions that join amino acids together
● Structure of R group affects how amino acid reacts with others in a protein molecule depending
on if the group is polar or not and will affect the tertiary structure
● R group should have a CH2 group
● Amino acids combine in a condensation reaction, peptide bond is formed CONH , dipeptide is the result
● When more and more aminos join , a polypeptide forms
● Protein is formed when polypeptide chain coils , folds or associates with another chain
● Peptide bond is very strong but other bonds are formed between amino acids in a chain and create the
3D structures of the protein. The bonds depend on R group and are - hydrogen , disulphide or ionic

Hydrogen bonds
● In amino acids there are tiny negative charge on O from COOH- and tiny positive charge from H in OH-
● Charged groups near in a polypeptide structure , opposite charges attract , form a hydrogen bond
● These are weak bonds but there are many of them , holding the protein together firmly
● Important in the folding and coiling of a polypeptide chain
● Bonds break easily and reform if pH or temperature conditions change

Reform- processing technique by which the molecular structure of a hydrocarbon is rearranged to alter its properties.

Disulphide bonds
● Form when 2 cysteine molecules are close in the polypeptide structure
● Oxidation reaction occurs between the 2 sulfur containing groups forming the covalent disulfide bond
● Stronger than H bonds but happen less often
 ● Important for holding folded polypeptide chains in place

cysteine (not needed to learn)

Ionic bonds
● Strongly positive and strongly negative amino acid side chains found deep inside protein molecule
● Strong bonds , not as common

● Straightening hair temporarily breaks hydrogen bonds

● Perming permanently breaks disulphide bonds

Protein structure
● Primary
● The sequence of amino acids that make up polypeptide chain and is held by peptide bonds
● Secondary
● Is the shape that the chain of amino acids folds into – either alpha helix or beta pleated sheet.
The shape is determined by the hydrogen bonding between the peptide bonds. Most fibrous
proteins have this structure.

● Tertiary
● The 3d shape of the protein , determined by the H,DIS,ION bonds between R groups of nearby
amino acids

● Quaternary
● Proteins have this structure when 2 or more polypeptide chains join together , sometimes with
the addition of the non protein prosthetic group. It describes how separate polypeptide chains fit
together in 3 dimensions
Denaturation - changes in pH and temperature affect the bonds keeping the 3D shapes of proteins in place ,
cause loss of shape and change the way they work

Fibrous proteins
● Long parallel polypeptide chains with occasional cross linkages causing fibers to form
● Insoluble in water
● Tough

Collagen
● Collagen is a fibrous protein of great strength due to presence of both hydrogen and covalent bonds in
its structure.
● Collagen molecules wrap around each other and form fibrils which form strong collagen fibers.
● Collagen forms the structure of bones, cartilage and connective tissue and is a main component of
tendons which connect muscles to bones.
● Fibers have a tensile strength similar to that of steel
● Very strong due to its unusual structure
● Primary structure - repeating sequences of glycine with 2 other amino acids
● Quaternary structure - 3 polypeptide alpha chains each upto 1000 amino acids long arranged in a
unique triple helix held together by hydrogen bond

Globular proteins
● Fold into spherical globular shapes
● Character of R groups on amino acids play imp role in its formation - Some r groups are hydrophobic-
repel water and some are hydrophilic- affinity to water
● Globular proteins are somewhat water-soluble - Carboxyl and amino ends give them ionic properties but
they are so large that they don't dissolve and instead form colloids (microscopic particles of one
substance suspended throughput another- they don't settle and can't be easily separated)
● Hold molecules in position in cytoplasm
● Examples - Antibodies , enzymes , hormones and hemoglobin

Hemoglobin

● Made up of 574 amino acids arranged in 4 pp chains joined by disulphide bonds. Each pp chain
surrounds an iron containing haem group which enables the hb to bind and release O2
molecules
● Arrangement of pp chain determines how easy the binding/releasing is
● Each pp chain contains 1 haem group which transports 1 oxygen molecule therefore one hb
transports 4 oxygen
Conjugated protein

● Protein molecules are conjugated to molecules called a prosthetic group

● Haemoglobins prosthetic group is iron
● Glycoproteins
● Prosthetic group is a carbohydrate
● Water holding ability and doesn't get broken down by proteases easily
● Lubricants in the body are glycoproteins - slippery and viscous , reduces friction
● Mucus in stomach protects the protein walls from digestion
● Lipoproteins
● Lipids are the prosthetic group
● Important in transport of cholesterol in blood
● Lipid part of molecule enables combining with cholesterol
● Two forms - LDls and HDLs - more proteins , more dense , more compact since proteins are
more compact than lipid

LDLs are the primary carriers of cholesterol in blood because their main role is to deliver cholesterol to both peripheral and
liver cells. In the process , these particles are modified and they accumulate in the arterial wall. HDL
carries LDL (bad) cholesterol away from the arteries and back to the liver, where the LDL is broken down and passed from
the body.

protei
ns
fibrou globu conju
s lar gated
colla haemo lipopr glycopro
gen globin otein
LDL/ tein
mucu
HDL s

Chapter 1B

https://www.youtube.com/watch?v=wgSUdxrlO8Y
The oxygen dissociation curve
Explaining the shape of the curve

○ Due to the shape of the hemoglobin molecule, it is difficult for the first oxygen molecule to bind
to haemoglobin; this means that binding of the first oxygen occurs slowly, explaining the
relatively shallow curve at the bottom left corner of the graph
○ After the first oxygen molecule binds to hemoglobin, the hemoglobin protein changes shape,
making it easier for the next hemoglobin molecules to bind; this speeds up binding of the
remaining oxygen molecules and explains the steeper part of the curve in the middle of the graph
■ The shape changes of hemoglobin leading to easier oxygen binding is known as
cooperative binding
○ As the hemoglobin molecule approaches saturation it takes longer for the fourth oxygen molecule
to bind due to the shortage of remaining binding sites, explaining the leveling off of the curve in
the top right corner of the graph

When the curve is read from left to right

● It provides information about the rate at which hemoglobin binds to oxygen at different partial pressures
of oxygen
 ○ At low pO2, in the bottom left corner of the graph, oxygen binds slowly to hemoglobin; this
means that hemoglobin cannot pick up oxygen and become saturated as blood passes through the
body's oxygen-depleted tissues
■ Haemoglobin has a low affinity for oxygen at low pO2, so saturation percentage is low
○ At medium pO2, in the central region of the graph, oxygen binds more easily to hemoglobin and
saturation increases quickly; at this point on the graph a small increase in pO2 causes a large
increase in hemoglobin saturation
○ At high pO2, in the top right corner of the graph, oxygen binds easily to hemoglobin; this means
that hemoglobin can pick up oxygen and become saturated as blood passes through the lungs
■ Haemoglobin has a high affinity for oxygen at high pO2, so saturation percentage is high
■ Note that at this point on the graph increasing the pO2 by a large amount only has a small
effect on the percentage saturation of hemoglobin; this is because most oxygen binding
sites on hemoglobin are already occupied

When read from right to left, the curve provides information about the rate at which hemoglobin
dissociates with oxygen at different partial pressures of oxygen

○ In the lungs, where pO2 is high, there is very little dissociation of oxygen from hemoglobin
○ At medium pO2, oxygen dissociates readily from hemoglobin, as shown by the steep region of the
curve; this region corresponds with the partial pressures of oxygen present in the respiring tissues
of the body, so ready release of oxygen is important for cellular respiration
■ At this point on the graph a small decrease in pO2 causes a large decrease in percentage
saturation of hemoglobin, leading to easy release of plenty of oxygen to the cells
○ At low pO2 dissociation slows again; there are few oxygen molecules left on the binding sites,
and the release of the final oxygen molecule becomes more difficult, in a similar way to the slow
binding of the first oxygen molecules

The Bohr effect

● Changes in the oxygen dissociation curve as a result of carbon dioxide levels are known as the Bohr
effect, or Bohr shift
● When the partial pressure of carbon dioxide in the blood is high, hemoglobin’s affinity for oxygen is
reduced
○ This is the case in respiring tissues, where cells are producing carbon dioxide as a waste product
of respiration
○ This occurs because CO2 lowers the pH of the blood
■ CO2 combines with water to form carbonic acid
■ Carbonic acid dissociates into hydrogen carbonate ions and hydrogen ions
■ Hydrogen ions bind to hemoglobin, causing the release of oxygen
● This is a helpful change because it means that hemoglobin gives up its oxygen more readily in the
respiring tissues where it is needed
● On a graph showing the dissociation curve, the curve shifts to the right when CO2 levels increase
○ This means that at any given partial pressure of oxygen, the percentage saturation of hemoglobin
is lower at higher levels of CO2
Fetal HB
● The hemoglobin of a developing fetus has a higher affinity for oxygen than adult hemoglobin
● This is vital as it allows a fetus to obtain oxygen from its mother's blood at the placenta
○ Fetal hemoglobin can bind to oxygen at low pO2
○ At this low pO2 the mother's hemoglobin is dissociating with oxygen
● On a dissociation curve graph, the curve for fetal hemoglobin shifts to the left of that for adult
hemoglobin
○ This means that at any given partial pressure of oxygen, fetal hemoglobin has a higher percentage
saturation than adult hemoglobin
● After birth, a baby begins to produce adult hemoglobin which gradually replaces fetal hemoglobin
 ○ This is important for the easy release of oxygen in the respiring tissues of a more metabolically
active individual

Artery diagram should show

{3 layers and endothelium} + lumen (1)
Tunica externa,tunica media , tunica interna , endothelium , lumen

muscle tissue contracts and elastic tissue stretches and recoils!

There is a delay between atrial systole and ventricular systole because

• because the atrioventricular valves have to close (before the
ventricles contract) (1)
• to prevent backflow of blood into the atria (1)

Chapter 2A
Membranes and transport

The cell surface membrane

● Forms the boundary of the cell
● Surround organelles
● Acts as a barrier , controlling what passes through the cell
● Allows fluids on either side to have different compositions allowing different areas to have different
conditions for different reactions
● Many chemical processes take place on membranes
● Must be flexible and allow the cell to change shape
● Vesicles combine with the membrane to release its contents

Its structure
Composed of phospholipids and proteins

Phospholipids
● 2 fatty acid tails joined to a phosphate group by a glycerol molecule - linked by ester bonds
● Are one of the polar lipids in the membrane , attached to a polar part - phosphate group
● Fatty acid chain - neutral , insoluble in water
● Phosphate group - negative charge , dissolves in water
● When in contact with water both parts of the molecule will react differently to form
○ Monolayer - hydrophobic fatty acid tails are in the air and phosphate heads in the water
○ Clusters called Micelles - hydrophilic heads point outwards and hydrophobic tails hidden inside
● Monolayer develops at the surface between air and water but In reality , water is always on both sides of
a membrane therefore bilayers are formed
○ Hydrophilic heads point inward and the hydrophobic tails are protected in the middle
○ This is called the unit membrane - basis of all membranes
● Allows fat soluble molecules to pass through but not ionic ones because they don't dissolve in lipids -
these enter cells because of proteins and other molecules
Fluid mosaic cell membrane model
● Current model of the structure of the cell membrane with the phospholipid bilayer as a fluid system with
proteins and other molecules floating within it
● The proportion of Phospholipids that contain unsaturated fatty acids affect how freely the protein
moves within the membrane
● Other lipids like cholesterol is a very rigid molecule so makes the cell stable and stronger making it
harder for small molecules and ions to pass, acting as a barrier
○ Less cholesterol protein movement isn't restricted and membrane fluidity increases

Proteins
● Proteins have a hydrophobic - buried in the lipid bilayer and hydrophilic part- involved in many activities
● Main function is helping substances move across the membrane
● Can make pores or channels that are permanent or temporary
○ Channels can be open / shut depending on cell conditions and are called gated channels
○ Pores may be active carrier systems using energy to move molecules
○ Pores may be gaps that allow substances to move in or out ; both directions
● Can act as specific receptor molecules
● May be enzymes , controlling reactions linked to the membrane
● Some are glycoproteins(carbohydrate prosthetic group of a conjugated protein) - important at the
surface of cells in the way cells recognize each other

*alcohols dissolve lipids

*high temperatures make lipids more fluid and can denature proteins

Movement of molecules through the cell membrane

Extra reading : factors that affect fluidity of the membrane

The length of the fatty acid tail impacts the fluidity of the membrane because the intermolecular interactions
between the phospholipid tails add rigidity to the membrane. The longer the phospholipid tails, the more
interactions between the tails are possible and the less fluid the membrane will be.

At lower temperatures, phospholipids in the bilayer do not have as much kinetic energy and they cluster
together more closely, increasing intermolecular interactions and decreasing membrane fluidity. At high
temperatures the phospholipids have enough kinetic energy to overcome the intermolecular forces holding
the membrane together, which increases membrane fluidity.

Cholesterol helps keep membrane fluidity from getting too high or too low at high and low temperatures.
Phospholipid tails can be saturated or unsaturated; refer to whether or not double bonds are present between
the carbons in the fatty acid tails. Saturated tails have no double bonds and as a result have straight, unkinked
tails. Unsaturated tails have double bonds and, as a result, have crooked, kinked tails. Saturated fatty acids
tails are arranged in a way that maximizes interactions between the tails. These interactions decrease bilayer
fluidity. Unsaturated fatty acids, on the other hand, have more distance between the tails and thus fewer
intermolecular interactions and more membrane fluidity.

Transport across membranes

● Affected by charge , size and solubility in lipids / water of the molecule

Passive transport
● When there is a concentration, pressure or electrochemical gradient
● No energy from cell required

1- Simple diffusion
● Movement of molecules of liquid/gas down a concentration gradient
● Movement due to random motion of molecules due to kinetic energy - affected by temperature
● If many molecules packed tightly together , random motion will make them spread out until they reach a
uniform distribution , but they will continue to move
● Small molecules like O2 and CO2 move through diffusion

2- Facilitated diffusion
● Substances with strong positive or negative charge / large molecules
● Involves proteins allowing specific molecules to pass down their concentration gradient

● Protein channels will allow specific substances to pass through it , based on their charge and shape eg.
sodium ion channels . Some channels (gated channels) only open if a particular molecule is present or if
there is an electrical charge across the membrane

● Protein carrier molecules will carry substances and are located on the cell membrane surface ; outside
surface if taking substance inside cell/organelle , inside surface if taking substance outside . Each
carrier will carry a specific molecule based on its shape, once it picks up the substance , it will rotate
through the membrane to the other side and change shape and release the substance. Process can only
take place down a concentration gradient

3- Osmosis
● Water potential measures the concentration of free water molecules not associated with solute
molecules
 ● Movement of water from region of high wp to a region of low wp down a wp gradient across a partially
permeable membrane
● Osmotic concentration - measure of the concentration of the solutes in solution that have an osmotic
effect - soluble particles , not large insoluble
● Three types of solutions
○ Isotonic - osmotic conc of solutes in solution same as cytoplasm in cells
○ Hypotonic(high wp) - osmotic conc of solute in solution lower than cytoplasm in cells
○ Hypertonic(low wp) - osmotic conc of solute in solution higher than cytoplasm in cells
*greater osmotic conc= lower wp

● Animal cells
○ Too much water moves in - cell bursts
○ Too much water moves out - cell shrivels up , cytoplasm loses internal structure

● Plant cells

○ When there is too much water in , the cytoplasm swells and pushes on the cell wall , creating
hydrostatic pressure . The cell wall pushes back against the cytoplasm creating a pressure
potential. Pressures cancel out the tendency of water molecules to move into the cell. The
osmotic force , moving water into the cell is balanced by the pressure potential forcing it out ,
making the cell rigid and in a state called turgor - supports the stem and leaf

○ Slightly hypertonic - water moves out , plant is less turgor , cell membrane pulls away from the
cell wall , protoplasm shrinks , incipient plasmolysis - 50% cells are plasmolysed and 50% are not

○ Hypertonic - so much water moves out , vacuole is reduced, protoplasm shrinks from the cell wall
completely - cells suffer plasmolysis

4 - Active transport
● process that involves the movement of molecules from a region of lower concentration to a region of
higher concentration against a gradient
 ● Involves a carrier protein , very specific and will pick up only one type of molecule or several similar
substances that compete with each other for a place on the carrier
● Energy needed is provided by molecules of ATP - used to move carrier systems or release the
substances
● Carrier system involves ATPase enzyme that catalyzes hydrolysis of ATP - breaking 1 bond and forming
2 more
● One way system for a specific substance , moving them in the direction required by the cell
● Move substances faster than diffusion

5 - When large particles need to enter or leave a cell - USES ENERGY

Endocytosis
● Movement of large molecules into the cell when membrane bound vesicles will surround and take up
materials due to vesicle formation
● Large scale eg. ingestion of bacteria - phagocytosis
● Small scale , tiny amounts of surrounding fluid taking into minute vacuoles - pinocytosis - very common
because cells take in fluids for nutrients or source of minerals

Exocytosis
● Movement of large molecules out of the cell by emptying of a membrane bound vesicle due to it fusing
with the cell surface membrane ; eg. hormones

Gas exchange systems

● Surface area to volume ratio is important in determining weather organism needs a mass transport
system to overcome limitations of diffusion to supply substances to the cells
 ● Organism gets bigger - sa/vol ratio gets smaller , organism needs specialized systems because
metabolic rate is higher , they are move active , control body temp etc
● Gas exchange in animals - lungs , in fish - gills , in insects - tracheal system , in plants - leaves
● Rate of diffusion is controlled by factors
○ Greater surface area , more particles exchanges , greater diffusion
○ Steeper conc gradient - faster diffusion
○ Shorter diffusion distance due to thickness of exchange surface - faster diffusion
○ Ficks law of diffusion - Rate of diffusion = surface area x concentration gradient / thickness of
gas exchange surface

● They all have certain features in common

○ Large surface area so that sufficient gas exchange takes place to supply all organisms needs
○ Thin layers to minimize diffusion distance
○ Rich blood supply to respiratory surfaces to maintain a steep concentration gradient
○ Moist surfaces
○ Permeable surfaces to allow free passage of respiratory gasses

Human gas exchange system - found within the chest , linked outside through the mouth and nose

1. Nasal cavity - passages of nasal cavity have a large surface area but no gas exchange takes place
here. The passage lining secretes mucus and is covered in hairs so that it filters out and removes dust ,
pathogens like bacteria and particles to protect lungs from infection and damage. Moist surfaces
increase water vapor in air and rich blood supply raises temperature so air entering lungs has little effect
as possible on internal environment
2. Mouth - air can enter through here but misses out on warming,moistening and cleaning
3. Epiglottis - flap of tissue that closes over the glottis in a reflex action when food is swallowed , preventing
it entering the gas exchange system
4. Larynx - voice box that uses flow of air across it , to produce sounds
5. Trachea - airway linked to the bronchi , lined with goblet cells which secrete mucus and have cilia which
moves mucus and trapped particles back up the throat
6. Bronchi - left and right bronchi - tubes leading to the lungs and divide to form bronchioles
7. Incomplete rings of cartilage - prevents the trachea and bronchi from collapsing and allows food to be
swallowed and moved down the esophagus
8. Bronchioles - small tubes spread through the lungs and end in the alveoli - some gas exchange may
take place here
9. Aleveloi - main site of gas exchange
10. Ribs - protective bony cage around the gas exchange system
11. Intercostal muscles - located between the ribs and are important in breathing- moves air into and out of
lungs maintaining steep concentration gradient for rapid gas exchange
12. Pleural membrane - surround the lungs and the chest cavity , forming a sealed and sterile unit
13. Pleural cavity - space between the membranes , filled with a thin layer of lubricating fluid called lung
surfactant- allows the membranes to slide easily with the breathing movements
14. Diaphragm - broad sheet of tissue made of tendon and muscle that forms the floor of the chest cavity
and is important in breathing movements

Alveoli
● Where gas exchange takes place
● is made up of a single layer of flattened epithelial cells
● Capillaries close to alveoli have a wall that is one cell thick
● Between the alveoli and capillaries is the elastic connective tissues holding everything together , allows
to force air out of lungs known as elastic recoil of lungs
● Macrophage is the WBC in alveoli that engulf bacteria , keeping the alveolus bacteria free
 ● Has a natural tendency to collapse which is prevented by the phospholipid that coats the alveoli making
breathing easier - Lung surfactant
● Gas exchange is the diffusion between the alveolar air and deoxygenated blood in capillaries
● Has a large surface area for exchange of gasses
● Blood is continuously flowing through nearby capillaries which maintains the conc gradient - air in alveoli
is constantly being refreshes with air from outside by breathing
● Walls of the alveoli and capillaries are only one cell thick , short diffusion distance - rapid and effective

Breathing
● Movement of air between lungs and external environment done through breathing / ventilation
● Breathing maintains the steep concentration gradient between the blood in capillaries and air in lungs
● Happens due to pressure changes in the chest cavity that bring about movements of air

● Inhalation is when the muscles surrounding the diaphragm contract pushing in downwards and flattening
it. External intercostal muscles of the ribs will also contract, raising it upwards and outwards. Volume in
chest cavity increases , pressure decreases . Pressure within the chest cavity is lower than pressure of
air outside so air is moved inwards to equalize pressure inside and out.

● Exhalation is when the muscles surrounding the diaphragm relax moving it into its resting domed shape.
External intercostal muscles relax so ribs move down and in , the elastic fibers around the alveoli return
to their normal length . Volume in chest cavity decrease , pressure increases- pressure in chest cavity is
more than outside so air moves out of lungs
● In forced exhalation , abdominal muscles contract , pushing the diaphragm upwards , the internal
intercostal muscles also contract , pushing the ribcage downwards eg. coughing

To reduce the chances of damage to the lungs , respiratory system produces a lot of mucus that lines the
airways and traps particles and organisms that is very runny so it is easily moved up by cilia that is swept
upwards back the throat- most mucus is swallowed and the acid in stomach and the digestive enzymes digest
mucus and everything carried in it.

Chapter 2B

Enzymes
Enzymes
● Biological catalysts that control the rate of reactions occurring in cells
● Make life possible by speeding up reactions in cells without changing the conditions of the cytoplasm
● Globular proteins
● Produced during protein synthesis when the mrna transcribed from the dna is translated
● Very specific shape due to their primary , secondary , tertiary and quaternary structures
● Show great specificity- catalyze only certain reactions or groups of molecules with similar shape - due to
their specific shape
● Inside cells - intracellular enzymes
● Outside cells - extracellular enzymes
● Named based on a recommended name usually short name of molecule that enzyme works on ,
systematic name describing the reaction being catalyzed eg.dna ligase or a classification number

How it works
★ Reacting molecules should have enough energy to break the bonds holding them together in order to
react
★ Active site has a specific shape due to the way the large protein is folded
 ● Enzymes lowers the activation energy needed for the reaction to take place

● Lock and key hypothesis - enzyme has an area called the active site that has a specific shape , only 1
substrate or type of substrate can fit. The formation of the enzyme-substrate complex lowers the Ae
because the active site affects the substrate bonds , making them easier to break. Once the products
are formed , the complex beaks up and the product is released

● Induced-fit hypothesis - active site has a distinctive shape which is flexible , after he substrate enters the
site , the shape is modified to from the active complex and once the products are released , the enzyme
returns to its inactive relaxed form for the next substrate

Enzyme activity

● Only small amounts of enzyme is needed to catalyze the reaction of many substrate molecules
● Turnover number - amount of substrate molecules transformed per minute by a single enzyme
● Increases the concentration of substrate will increase the rate of reaction until the enzyme becomes
saturated because all the active sites are occupied ; now only increasing enzyme concentration can
increase ror more

● Temperature - measure of the effect of temperature on a reaction is the temperature coefficient Q10
○ Enzyme catalyzed reactions in humans stops at 60 , at 40 most proteins lose their tertiary and
quat structures and denature - optimum temp is below 40
○ Thermophilic bacteria live in hot springs and works well at 85 because it is made up of
temperature resistant proteins containing high density of hydrogen and disulphide bonds

● pH
○ Affects shape of protein
○ Changes in pH affect formation of hydrogen and disulphide bonds
○ One way cells control effects of intracellular enzymes is to make small changes in PH to increase
or decrease their acidity

Anabolic reaction - build up new chemicals

Catabolic reactions - break substances down

Combination of this is called metabolism and the reactions of metabolism happen as a part of a sequence of
reactions known as a metabolic chain/pathway

DNA

★ Human cells are eukaryotes

Mono Nucleotides and polynucleotides

Mononucleotides

● Provide energy in form ATP

● Provide building blocks for mechanism of inheritance in form DNA and RNA

Has 3 parts
● A 5-carbon pentose sugar
○ In RNA it is ribose
 ○ In DNA it is deoxyribose
● Nitrogen containing base
○ Purine base - adenine and guanine (large molecules) PAG
○ Pyrimidine base - cytosine , thymine and uracil(smaller molecules)
● Phosphate group PO4 3-
○ The phosphate group means that the nucleotides are acidic molecules with a negative charge
● These three are joined by condensation reactions with the elimination of 2 water molecules , forming a
mononucleotide

Polynucleotides / Nucleic acids

● Carry all the information needed to make new cells

● These are polymers consisting of many monomer mononucleotide units
○ linked together by condensation reactions that produce phosphodiester bonds between the sugar
on one nucleotide and the phosphate group on the other
○ Polynucleotides therefore always have one hydroxyl group (from sugar) and a phosphate group
on either end

● RNA
○ Form single polynucleotide strands
○ Can either fold into complex shapes or remain as long thread like molecules

● DNA
○ Consist of 2 polynucleotide strands that twist around each other which results in a dna double
helix
○ Sugars and phosphate from the backbone of the molecule
○ Bases point inwards from the backbones and pair in specific ways - purine base pairs with
pyrimidine base
○ The two strands are held by the hydrogen bonds between the complementary base pairs -
between amino and carboxyl groups of purine/pyrimidine bases
○ 2 bonds between A and T , 3 bonds between C and G
○ For each complete turn of the helix there will be ten base pairs
DNA replication
Important feature of DNA is that it can replicate itself + also carry complex code , passing on genetic material
from one cell to another. There are a few ideas on how it replicates itself:

Conservative model

● Original double helix remains intact somehow instructs the formation of a new identical double helix ,
made up of entirely new material

Semi conservative model

● Assumes that the DNA unzips and new nucleotides align along each strand, therefore the new double
helix strands contains one strand of original dna and one strand made up of new material

1. DNA helicase breaks the hydrogen bonds between the two polynucleotide DNA strands causing the
double helix to unzip, forming two single strands.
2. Each original single strand then acts as a template for a new strand.
3. Free-floating DNA nucleotides join to the exposed bases on each original template strand via
complementary base pairing.
a. The nucleotides of the new strands are joined together by the enzyme DNA polymerase which
catalyzes condensation reactions to form a new strand. The new nucleotides are joined to the
template strand by pairing complementary bases; polymerase works from 3’ end to 5’ end of
DNA strand
b. DNA ligase joins the phosphate group of new nucleotide to (deoxyribose) sugar of growing
strand and forms phosphodiester bonds between them.
4. The original strand and the new strand joined together through hydrogen bonding between base pairs on
the original and new strand to form the new DNA molecule
5. Each new DNA molecule contains one strand from the original DNA molecule and one new strand and
the new molecules automatically coil up into the double helix structure

The genetic code

● Exists as a triplet code giving way for 64 different amino acid combinations- 20 of which are coded for
● These 20 amino acids combine to make an infinite variety of proteins through translation via the mRNA,
that happens on the surface of ribosomes
●
● Gene - sequence of bases on a DNA molecule coding for proteins that affect a characteristic in the
phenotype of an organism
●
● Each sequence of 3 bases code for an amino acid or to signal the beginning or end of a particular amino
acid sequence
● Sequence of 3 bases is called a codon
 ○ When figuring out the codons , the work was done on the mRNA because the DNA molecule was
too large.
○ The mRNA is formed as a complementary strand to the DNA therefore is like a reverse image of
the original base sequence
○ U replaces T eg. AAT on dna gives UUA on rna
● 98% of the human DNA is noncoding and these sequences are involved in regulating the coding
sequences , turning genes on or off
● Genetic code is a
○ Triplet code
○ Non-overlapping code
○ Degenerate code

Non-overlapping code

● Means that the triplets are read separately and there is no overlap between codons
● so each base on DNA is used in only one triplet codon
● Evidence suggested that it would be non overlapping if there was a point mutation(alteration of a
nucleotide) and only one amino acid is altered , which is what is seen in DNA
● This benefits the organism because only 1 amino acid gets altered in case of a point mutation

Degenerate code

● One amino acid is coded for by multiple codons

● Genetic code therefore contains more information than needed
● With a degenerate code , if the base in a triplet changed, the mutation can still produce the same amino
acid therefore it protects organism from the effects of a mutation
● Tryptophan and methionine(first AA in a polypeptide chain) are represented by a single codon

RNA

● Contains diff sugar than DNA - ribose

● Different base - Uracil instead of Thymine
● Consists of a single helix
● Does Not form complex molecules like DNA does
● Enables DNA to act as genetic material by carrying out 3 functions in the protein synthesis process and
3 diff rna do these tasks
1. Carries instructions for a polypeptide from DNA in nucleus to ribosomes where proteins are
made mrna
2. Picks up specific aa from protoplasm and carries to surface of ribosomes trna
3. Makes up the bulk of the ribosomes themselves rrna

In eukaryotes , the DNA that codes for individual proteins is in the nucleus and the proteins are synthesized at
the ribosomes in the cytoplasm. The RNAs (ribonucleic acid) carry the info from the DNA(deoxyribonucleic
acid) to the ribosomes

Protein synthesis

Transcription - dna transcribed to mrna

1. RNA polymerase binds to a specific sequence within the gene and pries the two strands apart
2. One strand is the is the sense strand which carries the code of the AA to be formed and the antisense
template strand is used to generate the mrna , reflecting the sense code on the dna
3. Beginning at the start codon , RNA nucleotides align along the exposed sequence of DNA bases in the
complementary fashion
4. RNA polymerase joins the chain of RNA nucleotides together and builds the mRNA until the chain
reaches the stop codon. (RNA polymerase catalyzes the formation of phosphodiester bonds between
the sugars and phosphate groups of the RNA nucleotides.)
 5. The mRNA separates from the DNA template and the RNA polymerase zips the DNA back up , it is
returned to its original state
6. Hydrogen bonds maintain the helical structure of the mRNA
7. The small mRNA molecules passes through the nuclear membrane easily and carries the instructions to
the cytoplasm where it finds the ribosome

Translation - mrna translated to form a protein

1. tRNA transfer rna found in the cytoplasm

a. One part has a 3 base sequence that determines to which piece of mRNA on the ribosomal
surface the tRNA will join - this sequence of 3 bases matches the genetic code of the DNA and
corresponds to one specific AA - called the anticodon
b. It also has a binding site that picks up one specific amino acid from the vast numbers free in the
cytoplasm
c. The anticodon will correspond to the amino acid that it holds
2. The tRNA molecules align beside the mRNA on the surface of the ribosome
3. Each mRNA codon codes for a specific anticodon carried by the tRNA - anticodons and the codons align
and are held in place by hydrogen bonds between corresponding bases
4. tRNA that corresponds to the next codon will enter the ribosome and it carries an amino acid that will
bind to the pervious amino acid from the start codon(methionine)
5. The first tRNA will now detach from the ribosome that has shifted over making space for the next tRNA
6. The new amino acid will bind to the previous two
7. This process continues in a sequence dictated by the codons on the mRNA , linking amino acids
together until the stop codon is reached , leaving a completed polypeptide chain
rRNA

● Ribosomal ribonucleic acid is a type of non-coding RNA which is the primary component of ribosomes (made
up of rRNA and proteins)
● Ribosomes surround and bind to parts of mRNA that are actively being translated and then move along to
the next codon
● Their job is to hold the mRNA and tRNA together and act as enzymes , controlling the protein synthesis
process

Mass production

● Cytoplasm contains polysomes - groups of ribosomes joined by mRNA threads

● Polysomes are used to mass produce some proteins
● Ribosomes attach to the mRNA and move along one after the other , producing identical polypeptides

Chapter 2C

Gene expression and genetics

Mutations

● Permanent change in the dna of an organism

● Point mutations
○ One or a small number of nucleotides miscopied during dna replication
○ Substitution - one base substitutes another
○ Deletion - one base is completely lost from the sequence
○ Insertion - an extra base is added to the sequence
● Chromosomal mutations
○ Changes in the position of the gene in a chromosome
● Whole chromosome mutation
○ The entire chromosome is lost or duplicated
○ Down syndrome is when the chromosome 21 has 3 copies instead of 2
● Usually occurs during DNA replication for cell division - Copying errors occur during the replication process,
wrong bases are inserted
● Cause problems like cancer and are very harmful when happen in gametes because it is passed on to future
offsprings

Effects of mutations

○ Usually don't have great effects because

■ Happen in non coding part of the DNA
■ Code is degenerate , change in the codon does not alter the amino acid being made
○ Produces variation- sometimes a new superior protein is produced giving a reproductive advantage
○ Neutral mutations are some that don't worsen or make chances of survival better , no effect
○ Some mutations cause great damage - if the mutation is in a protein that has an important function of
a cell example active site of an enzyme
● In gametes - cause genetic diseases
● In somatic cells - different types of cancer
● Mutagens - anything that increases the chances / the rate at which a mutation may occur eg. X rays , ionizing
radiation, certain chemicals

Sickle cell disease

● Genetic disease affecting the protein chains of Hb in red blood cells
● Result of point mutation
○ Change in the base of one codon changes a single amino acid in a chain of 147 amino acids but
this change alters the nature of the protein
○ GAG codes for Glu - GTG codes for Val
● The Hb molecules stick together forming rigid rods , giving the rbc a sickle shape
● Can't carry o2 efficiently , prevents blood flowing through capillaries
● Causes severe pain , can cause death

Patterns of Inheritance
 ● Phenotype - the physical traits making up the appearance of an organism , partly the result of the
genotype passed from parents to offspring and partly from effects of the environment the organism lives
in

● Genotype - genetic makeup of an organism with regards to a particular feature. Differences of

genotype between individuals of the same species is due to
○ Rearrangement of genes during meiosis
○ Inheritance of genes from 2 diff individuals in sexual reproduction

● Homologous pairs - matching pairs of chromosomes that contain the same genes but possibly
different alleles. Half the chromosomes are inherited from the female parents and the other half from
the male parent- two sets are arranged as matching pairs called HP

● Along each chromosome are hundreds of genes and each gene is a diff segment of DNA coding for a
particular polypeptide or protein. Chromosomes in a homologous pair carry the same genes and
the gene for a particular character is found in the same position / locus; you have two genes for
one characteristic. Each gene exists in slightly diff versions called alleles

● Locus - site of a gene on the chromosome

● Alleles- versions of the same gene

○ If two alleles coding for a characteristic are identical - homozygous for that characteristic , it is
called a homozygote , if the alleles are different - heterozygous for that characteristic and is
called a heterozygote
● Some phenotypes are recessive some are dominant
○ Recessive - characteristic which is only expressed if both alleles code for it
○ Dominant- characteristic which is expressed whether the individual is homo or heterozygous for
that allele

True breeding - homozygous organism that will always produce the same offspring when crossed with another
true breeding organism for the same characteristics. Heterozygotes are not true breeding - when crossed ,
offspring has at least 2 diff phenotypes

Monohybrid cross
● When genes are considered individually in a genetic cross / when only one gene for a characteristic is
considered - it is called a monohybrid cross.
● Crosses are represented using diagrams called punnett squares.
● It shows you the potential alleles inherited from parents and the potential resulting offspring.
● First generation of the cross is the F1 and if we cross individuals from the F1 generation , the next
generation is the F2 ( first filial and second filial generation)
Test crosses
● Used by breeders
● If a feature is a recessive phenotype , any organism showing that feature is homozygous.
● For features with a dominant phenotype , physical appearance wont show homozygous or heterozygous
● To find out if it is homo or hetero , the individual needs to be crossed with a homo recessive individual
● This type of cross is a test cross and will reveal the parental genotype

Genetic Pedigree Diagrams

● Shows how a trait can be theoretically passed on and the probability that a different offspring is
produced. It shows what happens over a long period of time , it includes the sex of the individuals , all
the members of the family and whether or not they have a particular characteristic or disease
● Highlight carriers of a recessive phenotype- useful for families affected by conditions so is used to
predict carriers of a genetic mutation- allows people to consider options b4 having a child
● Useful for identifying sex - linked traits
● Tracks mutations

Codominance
● When both alleles at a gene locus are fully expressed in the phenotype
● In the humans there is the ABO blood group system
○ Three alleles - IA IB IO which code for the presence or absence of antigens on the surface of red
blood cells
○ A - a antigens, dominant
○ B- b antigens , dominant
○ O- no antigens , recessive

Sampling errors
Theoratic ratios of phenotypes from genetic crosses that are predicted are usually never precise - reproduction
is a result of chance and combination of alleles is random , some offspring die before they can be sampled.
Smaller the sample , larger the sampling errors - organisms like bacteria , fungi and fast growing plants are
useful because they produce large numbers quickly

Autosomes - the autosomes are all the homologous pairs of chromosomes except the sex-linked ones, which
are controlled by the sex chromosomes. They carry information about the cells. In humans there are 22 pairs of
autosomes and one pair of sex chromosomes
Sex chromosomes - X and Y chromosomes and carry information about the sex of the individual
Homogametic - female has two X chromosomes in her gametes
Heterogametic - males have one X and one Y chromosome in his gametes
Y chromosome - 23 million base pairs , carries male sex information
X chromosome - much bigger with 150 million base pairs , codes for all female characteristics , carries genes
coding for traits like blood clotting and ability to distinguish colors

Sex linked genes - gene for particular charecteristic located on the sex chromosome. Genes carried on X
chromosome will be expressed even if recessive , if passed on from female to male because there is no
corresponding allele on the Y chromosome

Sex linked diseases

Mother always donates X chromosome to her son and any mutations in genes on the X chromosome , affects
the phenotype of offspring even if it is recessive. Sex linkage leads to sex linked diseases
● Red green colorblindness
○ Ability to see in color results from the genes that code for particular proteins allowing this - genes
located on X chromosome , recessive mutations in these genes affect our ability to see in color
○ More common in men because the have only 1 X chromosome , if that has the RGCB gene from
the mom , they will also have it - that's why we say condition is SEX LINKED
● Hemophilia - found only in boys
○ Components of blood clotting process are coded for by genes , some located on X chromosome,
when protein needed for blood clotting is missing - hemophilia result
○ Most common form is when clotting factor VIII is missing
○ The homozygous form is dangerous - female fetuses affected won't survive birth and untreated
males can have small injuries that lead to death due to excessive bleeding
○ In the past treated by blood transfusions or extracting clotting factor VIII from donated blood ,
now recombinant bacteria produce it in large quantities

● Cystic fibrosis
○ Severe genetic disease
○ To summarize : important membrane transport systems gets damaged because of a faulty
recessive allele - the chloride transport systems of the exocrine gland don't function properly
leading to production of thick sticky mucus
○ The CFTR ( cystic fibrosis transmembrane regulatory) protein lines the channels through which
chloride ions leave epithelial cells and move into the fluid outside cells in the lungs
○ CFTR protein is enormous and the gene coding for it is found on chromosome 7
○ Mutation in any part of this gene affects the CFTR protein , causing CF
○ 1000 diff mutations in this gene have been discovered , all coding for a faulty CFTR protein
○ All mutations are recessive but people who inherit TWO copies of the faulty allele will lack the
effective CFTR protein
○ Chloride ions build up in cells instead of moving out through the channel , water doesn't move
out of the cells to dilute the mucus on the membrane surfaces.
○ Water moves into cells by osmosis from fluid surrounding the cells , making the mucus more
thick and sticky
○ Diffusion of gasses is much slower due to the thick mucus layer between blood and air , reduces
air flow in and out of lungs - diffusion distance is less steep
○ Since it is caused by a recessive allele many people are carriers and are phenotypically normal-
problems shown only if 2 carriers have children together but since it is recessive there is only a 1
in 4 chance that the child will develop CF

○ Respiratory system
➔ Mucus builds up in the airways of the lungs , reducing flow of air into alveoli and obstructs
the bronchioles completely , preventing air flow into bronchioles
 ➔ Smaller concentration gradient between air and blood in the lungs -reduces gas
exchange
➔ Mucus reduces surface area for gas exchange
➔ Individuals have severe coughing fits as the body tries to expel the mucus
➔ Feel breathlessness and are short of oxygen so feel tired and lack energy
➔ Mucus is so thick and sticky that cillia cannot move it along and out the system so the
lungs fill up with mucus , less effective gas exchange
➔ Bacteria and pathogens trapped in mucus builds up , bacteria breeds in the ideal
conditions and grows
➔ Body normally secretes antibodies into mucus to inactivate pathogens but in CF the
chemical balance of mucus is changed as water is moved out of mucus into cells making
the solutes more concentrated - dehydrated surfaces of cells lose their antibacterial
properties as WBC and antibodies cant function effectively
● Can be restored if they are rehydrated

○ Digestive system
➔ Makes enzymes breaking down large food molecules into smaller ones- pancreas makes
some of the vital enzymes that move into the duodenum along the pancreatic duct
➔ Faulty CFTR protein - mucus in pancreatic duct is thick and sticky , blocks the duct ,
enzymes don't reach duodenum
➔ Cannot digest food properly , no enzymes - less nutrients
➔ Enzymes trapped in pancreas digest and damage pancreatic cells- may affect cells that
make insulin - cause diabetes
➔ Makes it difficult for food to be absorbed into the blood because mucus forms a barrier
between intestine lining and gut contents , reducing absorption surface area - malnutrition
risk

○ Reproductive system
➔ Women with CF will produce eggs but mucus blocks the cervix so sperm cant reach the
eggs or mucus blocks oviducts , fertilization cant happen
➔ Men with CF are infertile , tube carrying sperm out from testes to semen is not present /
tube is blocked by mucus

○ Sweat glands
➔ For people that have CF , their sweat is more concentrated and salty
➔ Reabsorption of salt prevents us losing too much salt in the sweat but without functioning
CFTR protein , chloride and sodium ions remain in sweat so it is very salty
➔ Na and CL levels are important for the nervous system and if too much salt is lost the
conc of body fluids change which can affect the heart
➔ electrolyte (salt) balance is upset. This affects the contraction of the muscles, the heart,
the nervous system, the kidneys, movement into and out of cells by osmosis – the whole
way the body works is less efficient.
➔ Salty sweat in babies = early warning sign to doctors

Genetic screening - whole populations tested for a genetic disease

Phenylketonuria
● Genetic condition - Recessive autosomal disease
● Body lacks enzyme needed to digest phenylalanine amino acid , the amino acid builds up in the blood
● Irreversible damage to brain and nervous system , if babies are diagnosed after birth , given diet free of
phenylalanine
3 options for parents - hope they are lucky their child has healthy genes , decide not to have children to
prevent passing on a faulty gene or do prenatal screening

Prenatal screening - used to try and discover if a fetus is affected by a serious condition , early in the
pregnancy , carried out on fetal cells collected from mother, after cells are obtained , karyotyping DNA analysis
takes place

1. Amniocentesis
○ Removing 20cm3 of the amniotic fluid surrounding the fetus using syringe and needle
○ Done at 16th week of pregnancy
○ Fetal epithelial cells are recovered from fluid by spinning in centrifuge
○ Cells cultured for 2-3 weeks
○ 1% risk of spontaneous abortion (miscarriage)
2. Chorionic villus sampling
○ Sample of embryonic tissue taken from placenta
○ Bigger sample of fetal tissue available for sampling
○ Done at 8th week of pregnancy
○ Faster results
○ 1% risk the embryo may spontaneously abort after the tissue sample is taken
○ Paternal X chromosomes are inactive in fetal placental cells so problems in these genes aren't
detected
○

Amniocentesis Chorionic villus sampling

Amniotic fluid Embryonic Placent

tissue a
Fetal epithelial Fetal placental
cells cells

Preimplantation genetic screening

● It is a technique which is based on the technique of IVF
● Egg and sperm fertilized outside the body , single cell removed from each embryo
● No harm caused to embryo development
● Genetic makeup is checked and only embryos free of problem alleles places into mothers uterus to
implant and grow
● Easy removal of faulty allele from gene pool

Genetic counseling - trained to help people come to terms with their situation of carrying faulty allele that can
cause genetic disease , how to move forward based on their own framework of moral , social , religious and
family beliefs

the ethical issues relating to genetic screening

screening may result in {an abortion /taking a human life} that is {unethical / against religious or cultural beliefs of
some people} (1) • spare embryos from IVF are destroyed which is taking a human life (1) • individuals who are
genetically linked may be {exposed to unwanted facts / disadvantaged} following testing (1) • screening may produce
false results or {CVS / amniocentesis} increases risk of miscarriage (which results in death of fetus)

Common questions
How a mutation for a gene affects the protein - There is a change to the sequence of nucleotide base pairs/triplets of
bases in the DNA/gene. This leads to a change in the sequence of codons in the mRNA at transcription and so,
during translation, there is a change to the sequence of amino acids assembled. This is therefore a change to the
primary structure of the CFTR protein, which leads to it not being able to fold into its correct tertiary structure.

How non functioning CFTR protein leads to CF - The non-functioning (wrong tertiary structure) proteins form chloride
ion channels that are not the correct shape and so do not transport chloride ions across the membrane, out of the
epithelial cells. This leads to lack of sodium ions leaving the epithelial cells and subsequently not enough water
leaving the cells by osmosis, so there is not enough water in the mucus secreted by the goblet cells. The thick, sticky
mucus is difficult to be moved by the cilia (which also lack hydration), so it builds up in the airways leading to
difficulties with gaseous exchange and the pathogens trapped in it stay in the airways and cause infections. This
accumulation of thick, sticky mucus also happens in the digestive and reproductive tracts. It can lead to infertility and
lack of absorption of digested food.