bbiioollooggiiccaak mmookeecakeess

what are monosaccharides

monosaccharides are monomers of carbohydrates and have the
smaller unit
general formula CH20 n theyre groupedbased on the numberof carbon
atoms called

trio se 3C pentose SC hexose GC

they are all sweettasting soluble in water and formcrystals but more known
as reducingsugarsmeaning

they can donate electrons to reduce another chemical

examples include Glucose Fructose Ribose and Galactose all hexose

how is glucose adapted forit'sfunction

Glucoseforms 2 isomers known as a glucose and B glucose which gives
themdifferentproperties

OH OH
CHz CHz

C C H C C OH
H H
C c C c
OH H
OH C C OH C C

H OH It OH

Alpha Beta
how do we test for reducing sugars
We use a Benedicts Test
1 grindfoodsample with water
2 add 2cm of Liquidfoodsample
3 add 2cm benedicts reagent
4 heat in water bathfor 5minutes
5 positivetest gives a brick red percipitate

Whydoes this test work

reducingsugarsconvert thebenedicts copper Il Sulphate intocopper1 oxide as
when heated copper Il ions acceptelectronfromsugar toform copper 1 which is
red

what are monosaccharides used for

In general monosaccharides provide quickenergy for the body tofunction

act as respiratory substrate

provide building blocksforlargercarbohydrate molecules

glucoseC50010 is hypertonic and can providecalories in minimal water

Can restore blood glucose concentration

pentose used for ATP synthesis

hexose is a source of energy by cell respiration
what are disaccharides
disaccharidesformwhen 2monosaccharidesform a glycosidic bondthroughcondensation
reactions and water is removed

They are watersolubledue to the manyhydroxyl groups sweettasting andquitepolar

since theyrequitelargemolecules theycan'tcross cell membranes which is why
they'rehydrolysed to form monosaccharides

the commonexamples are i

maltose Sucrose Lactose
most of them are non reducing sugars i
cannot donate electrons

how do we test for non reducing sugars

1 add 2cm's liquidfoodsample
2 add 2cm's dilute HCl

3 heat in water bath for 5minutes

4 add sodium hydrogencarbonate to neutralise use PHpaper

5 complete Benedicts test

6 if non reducing then turns orangebrown
What are the properties and uses ofdisaccharides
Sugar Properties Sources Uses Digestion

glucose fructose fruits a table sugar

In small
sweeter than glucose hectors sweetening intestine
sucrose soluble in water
agent sucrase
sugar cane
making inverted
white crystalline solid sugarsyrup invertase

non reducing
glucose galactose
mammary infant formula In small
less soluble than glands of as sugar intestine
sucrose mammals
lactase pharmaceutical lactase
less sweet than a
milk industry as
sucrose ingredient
white crystalline
solid

glucose glucose malt o hard candies In small

intestine
maltose reducing sugar product of a cheap
starch digestion sweetener maltase
soluble in water

sweet taste
 what are polysaccharides

Polysaccharides are polymers of many monosaccharides and formed via

condensation reactions The three key ones to know are

starch cellulose glycogen

and theyre all non reducing sugars

what is starch

Starch is a majorglucose storagecompoundfound in plants in theform of granules

and made up of 2 components

1 an amylose polysaccharide of a glucosemonomerswhich is unbranched with a linear

chain which spirals as it lengthens so its more compact and makes up 20 30010
of starch Themonomers are joined by 1,4 glycosidicbonds and the whole shape
is held by hydrogen bonds
2 an amylopectinpolysaccharide of a glucosemonomerswhicharejoinedby 1 4 and
I G glycosidicbonds The l G form links which make branches so it gives it a
largersurfacearea forenzymes and makes up 70 8040 of starch

what are thepropertiesofstarch

It is insoluble because its a largemolecule so can bestored within cells and not
dissolve so it can't affect cell water potential

spiraling of amylose makes it compact so can fit in small places

amylopectin branching giveslargesurface area for easyhydrolysis

quick hydrolysis means it can provide a rapid supply of energy

amylase hydrolyses slower so releases energy over a longer period of time
 What is cellulose
Cellulose is a polysaccharide made up of B glucose monomers and is located
in the cell wall of plants to provide structure and strength and has the structure

Unbranched 1,4 glycosidic bonds

long straight parallel chains of B glucose held together by many

hydrogen bonds also makes it strong

inversion of alternate glucose molecules

what is cellulose microfibril

microfibrils are made up of 60 70 cellulosemolecules which form cellulose fibres
they are

a
flexible
contain parallel arrangement of cellulose chains

what are the properties of cellulose

Unbranched 1.4 Chains are long and provide strength via the hydrogen
bonds
theyform microfibrils which also provide strength and flexibility
this prevents the cell wall frombursting due to osmatic gain or loss
hydrogenbonds are hard to break
resists action of enzymes
 What is glycogen
glycogen is a polysaccharide made up of a glucose held by 1 4 and branched l G
glycosidic bonds and is found as a storageproduct ofanimals as small granules in
the liver and muscles Its morebranchedthan amylopectin

What are the properties of glycogen

It is insoluble because its a largemolecule so can bestored within cells and n
dissolve so it can't affect cell water potential

branching giveslargesurface area for easyhydrolysis

quick hydrolysis means it can provide a rapid supply of energy

good for animals as they have a higher metabolic rate and need more
glucose

can we test for polysaccharides

the presence ofstarch can be confirmed by addingiodine to a liquid food
sample If positive it turns blue black

the presence of cellulose can be confirmed by adding Schulze reagent to

sample If positive it turns purple
what are lipids

Lipids are non polar molecules that are insoluble in water but dissolve in ethanol
and made up of fatty acids and glycerol that don'tform polymers examples
include
triglycerides phospholipids waxes

what are triglycerides

triglycerides are made up of 3fatty acids and I glycerol molecule which are
bonded via a condensation reaction

what are saturated vs unsaturatedfatty acids

Saturated have no double bonds so have straight shape thats tightly
packed in parallel so often solid fat
Unsaturated have 1 or more double bonds which Kinks making a less straight
chain thats furtherapart so in liquid state coils
how does the structure of triglyceride result in its properties

many C H bonds act as energystorage

hydrophobic so won't affect cell water potential

low in mass so can be storedwithoutpreventing animal movement

what are phospholipids

phospholipids are made up
and arranged as
of 2 fatty acids glycerol and a phosphate molecule

hydrophilic head which interacts

with water not fat
hydrophobic tail which interacts with
f at but moves awayfrom water

what is a phospholipid bilayer

When in water a bilayerforms to prevent water soluble solutionsfrom entering
so they're used as memebranes as they direct solutions to certain channels
how is the phospholipid adapted to its properties

polar molecule as it has hydrophilic head and phobic tail

when in water they move so onlyheads are exposed to water

bilayerforms around cells

enables surface ofplasma membrane to stay in place

receptors can form on

bilayer
what are waxes

waxes are made up of esters of fatty acid chains and alcohols which are
hydrophobic and inert due to their saturatedhydrocarbon chain
O

what are the roles oflipids

creating plasmamembrane
energy source when oxidised

protection of delicate organs

insulation as fat slowlyconductsheat

waterproofing due to insolubility

what is the test for lipids

2cm of liquid food Sample
2cm of ethanol
must shake to dissolve ethanol
add 2cm of distilled water

If positive a Milky percipitate forms

 what are protiers
protiers are macromolecules made up of amino acids of which there are 20
that have the structure Rgroup
H
1 HO
N C c
n
H H 0

theyjointogether via a reaction between one amino group and one carboxylic
group to form a peptide link

thestructureofprotiers
protienshave highmolecularweight and made upof amino acids which link
together via peptidebonds into a polypeptide chain Sometimes a singlepolypeptide
chain is a functionalprotier but we can link them togethertogether

primary structure
the sequence ofamino acids in a polypeptide chain

this determines the number kind and arrangement of amino acid forming protien
Carboxyl and amine groupformpeptide bonds
 Secondary structure
the sequence of amino acids causes parts of the protienmolecule to bend into either
an alpha helix coil held byhydrogenbonds in the same direction as the coil

a beta helix which is a pleatedsheet in an S shapepatternalso held by H bonds

tertiary structure
secondarystructure is bent and folded to form a precise 3Dshape which is held
by
hydrogenbonds polar 12 group polar 12group
disulphidebonds between R groupsof 2 aminoacids containing sulphur
ionic bonds positively charged 12 groups together
hydrophobic interactions amino acids point towards polypeptide

hydrophilic interactions amino acids point outward towards water

 Quaternary structure
madeupofmultiplepolypeptidechains theyrefolded into a 3D structure and held
by the hydrogen ionic and disulphidebonds They maycontain a prostheticgroup
which is a non protier groupattached to protier

the link between denaturing andprotierfolding

each protier has a uniqueshape

change in enviormertcausesprotierto lose 3Dstructure andturninto string of aninos

primarysequence not lost only structure

its now denatured and nonfunctional
note in rare cases we canreversethis byreturning to originalenviormentsince the
original sequence wasnt lost

fibrous protiers
Made up of long twistedstrandsof polypeptides they provide a structuralrole
and are
insoluble dueto highproportion of hydrophobic R groups in amino acids

Strong rigid
stable
e
g keratin i many di sulphidebonds so less flexible

collagen flexible 1 tear resistant

 f
Globular protiers
Made up of polypeptide chain that is folded into a sphericalshape and
providefunctional roles as theyre
Water soluble hydrophilic R groups face outwards and vice versa
more sensitive to enviornert charge
irregular amino acid sequence
eg
Enzymes Haemoglobin insulin

how do we test for protiers

2cm of liquidfood sample
2cm of sodium hydroxide
2cm of copper sulphate

If positive turns purple

 bbiiooehheemmiieaatrreeaaettiioonss.in aeekkss

what is an enzyme

an enzyme is a globularprotien which acts as a biological catalyst

by altering
the rate of a chemical reaction without undergoing any permanent changes so
to
they can bereusedTheybasically create alternate pathways speed up reactions
how are they structured

enzymes are globular with specificlarge 3D structures but only a small section of
them isfunctional called the active site which is a small hollow depression within
the molecule

active site
i i
active
site
en
emo

howenzymes work via the lock and key model

Sinceenzymes are specific this model suggeststheyre locks and a fixed shape
while the substrate is a complimentary key
when the substratecollideswith active site
f
Gfq MBA
199
IA
gf5sfffff
fftq.IT it creates an enzyme substrate complex
whichdistorts the substrate and lowers the
activation energy

the products are then released and enzyme can be used again

howenzymes work via the induced fit model

Sinceenzymes are specific this model suggeststheyre gloves while the substrate
is a hand so the site will mould to become completly complimentary to the
substrate

ummm As
when the enzyme substrate complex
YBARRA UBBBVM.TT
occurs the mouldingputs a strain
on the bonds and lowers activation
energy

Products are then removed and active site returns to

original shape
 what factors affect enzymes
Sincetheyreprotiers theyre more sensitive to certain conditions
temperature PH Substrate enzyme concentration

whyis temperature important

the increase oftemperature increases kinetic energy of molecules therefore
molecules move more rapidly and with more energy
and have more succesfulCollisions optimal 37 40 C

if too high their enzymes can be denatured

and fail to work C 60 C

if too low then enzyme activity lowers and stops

completly at 0 C

whyis PH important
Enzymes are protiers so any PHchange can affect the hydrogen and ionic
bonds of NHz and coat which can alter the active site shape
It can also alter the charges of amino acids so substrate can't join

if toohigh then enzymes can denature and won't

work

if too low thenenzymeactivity towers until its also

denatured

whyis substrate enzyme concentration important

Substrate concentration enzyme concentration

increasing conc increases the
rate of reaction
but onceall enzymes are bound
then addingmore has no affect
all enzymes are saturated and
working at their maximum rate
increasing conc increases the
speed of reaction
but once all substrates are bound
then addingmore has no affect
all enzymes are saturated and
working at their maximum rate
What are enzyme inhibitors

an enzyme inhibitor reduces the rate of an enzymecatalysedreaction by

interfering with the enzyme this may be temporary or and
permanent there are
2 main types

Competitive non competitive

how do competitive inhibitors work

Usually temporary theseprevent the formation of the enzyme substrate

complex bytaking the place of the substrate
9 sotheyfit the active site but remain
unreacted as theyre a differenttype
of structure

this decreasesenzymeactivity as less substrates are able to bind which also

decreases rate of reaction

since this istemporary the level of

T
inhibition depends on the relative
concentration of substrate to inhibitor as
theyre competing for the active site

how do non competitive inhibitors work

these work to prevent the formation of products by the substrate so they
attach to a non active site called the allosteric site

this distorts the 3D tertiary

µ structure of the enzyme so
fj the active site charges and
substrate cannot bind

this isn't affected by substrate concentration and is

usually permanent
to
go

ft
SM
why do we need enzyme inhibitors

they serve many purpouses but are often used to treat disease drugs
or in agriculture as pesticides
E g competitive inhibitor Relenza

so relenza binds to the neuraminidase active site so virions are not

released from infected cells stopping the spread of influenza virus

eg non competitive cyanide

cyanide poison which prevents ATP birds to allosertic site to

alter active site which means cytochrome oxidase can't pass electrons
to oxygen
electron transport chain cannot continue to function and ATP is NOT
produced
why are enzymes needed for our metabolism
Our metabolism is the total of all reactions that occur within us to maintain
life and usually result from a series
of pathways which are controlled by
specificenzymes
what are metabolic pathways
metabolicpathways allow for a greater level of regulation andtypically are organised
into chains or cycles of enzyme controlled reactions
eg glycolysis or Krebs cycle
 transport inn and nut of Geeks
understanding the membrane
all membranes have the same basic structure known as the plasma membranes

how is theplasmamembrane structured

bilayerofphospholipids
protiers are embedded into the
bilayer in 2 ways
extrinsicprotiens on the surface
and don'textend across
badoo.TT
tSB
intrinsicproliers spanacross the taffies
bilayerfromside to side
Cholestrolmay be present to restrict the lateralmovement of other molecules

carbohydrates are attached to protiers or lipids on the outer side of the

membrane

whyis the structure called the fluid mosaic model

thephospholipidbilayer can move which makes the structureflexible andconstantly

changing shape like a
fluid
as the protiers embedded are differentshapes sizes and palterened randomly
theyappear like a mosaic

what is the function of the individual components of the plasma membrane

1 Phospholipid bilayer

allows lipid soluble substances to leave and enter cell

makes itflexible

prevent water soluble substances to leave and enter cell

een see
2 extrinsicprotiers

give mechanical support to membrane

can make glycoprotiers and glycolipids

can act as receptors for cell recognition

3 instrinsicprotiens

theyformtransportsystems formolecules
can be an enzyme

give mechanical support to membrane

4 Cholesterol

It stablizes the membrane bylimiting phospholipid movement

 what is diffusion

diffusionis the net movement ofparticles from an area of highconcentration to an area

of low concentration across a concentration gradient in a passive way

o o
o O o
o o o o o
e o
00 o
B o
o B o
o o o o
o o o
o o o

what affectsthe rate ofdiffusion

1 concentration gradient

thegreaterthe difference the quicker the rate

2 temperature

thehigher thetemperature the more kinetic energy sofaster rate

3 area

a largersurface area means quicker rate

diffusion
4 thickness surface difference in
of exchangesurface area concentration
a thinnersurface means faster rate
length of diffusion path
5 Size of particle
smallermoleculesdiffusefaster

6 Solubility of particles

fat solubles diffusefaster than watersoluble molecules

 What isfacilitateddiffusion

diffusionis the net movement ofparticlesfrom an area of highconcentration to an area

of low concentration across a concentration gradientvia the aid of a membrane
protien in a passive process

which membraneprotiers are used

I carrierprotiens

onlybinds specific molecules via an attachment

like enzymes
Slower rate of transport
also used in active transport
e g movesglucose in body

2 ChannelProtiens i

ion selective
can be gated toregulatepassage of ions

fasterrate oftransport
form waterfilledtubes for soluble ions

what are examples in the body

Potassium Channels

sodium potassiumpump carrier protien

 What is osmosis
Osmosis is the net movement of water molecules from an area of highwater potential
to an area of low water potential across a partially permeable membrane until
equilibrium is reached in a passive way

what is waterpotential
Waterpotential measures the concentration offree water molecules the more there
are the higher the water potential

1 pure water zero highest value

waterpotential in cells
Cemal J low
high
water water potential
potential
 What is activetransport
activetransport is the net movement ofparticles from an area of low concentration
to an area ofhigh concentration against a concentration gradientbyusingenergy
and carrierprotiers

how is the energy generated

Primaryactivetransport uses directhydrolysis of ATP

ATP H2O ADP 1 phosphate 1 energy

 how does active transport work
I carrier protier pump opens to theinside of the cell

2 pumpbinds to particle

3 bindingtriggerspump to hydrolyze ATP

7 ADP t
4 ATP H2O Pi t E

S protien molecule changes shape and points to opposite side of membrane

6 particles are released to other side of membrane

7 phosphate released to recombine with ADP to form ATP

8 protier reverts to originalshape

9 cycle repeats

e g sodium potassiumpump

i
r

p r

s
s l
t
 What is co transport
this is known as secondary active transport as it uses a differentsource of energy
where does this energycomefrom

energyfromprimary can be stored within electrochemical gradient

Secondary uses this energy to move other substances against their own
gradient at the same time sharing

how does cotransport work

Movement particle is coupled to the uphill transport
of of other substances by
Sharing carrier prolier l a cotransporter
a

l
if they move in same directiontheyre
Symports
2 opposites are anti ports

B F bn
example

Ht Ht Ht

Ht Ht
Ht

Ht Ht

Ht
 ggaasseexxehhaanngg.ee

how is the gasexchange system structured in insects

insects are terrestrial and very small organisms with an almost impermeable
exoskeleton and have no transportsystemwhich is whygases must be directly
transported to respiringtissues Instead they have a tracheal system

spiracles
these are tiny holes on the insectexoskeleton
which lead to a network tubes and can be
of
closed by values and surrounded by tiny hairs

trachea
these are supportedby strengthed rings to prevent
themfromcollapsing and branchfurther
air sacs
theseincreaserespiratoryefficiency byproviding a larger surface area
tracheoles
the smallest tubes these extend throughout all of the body tissues and also
contain small amountsoffluid in which gases are dissolved

muscle cell

the fluid is drawn into the cells and tissues

how dogasesmove in the tracheal system

1
Using a diffusiongradient
cells respire

Oz is used up and concentration falls near tracheoles

more 02 outside insect than in tracheal

diffusiongradient occurs and Oz enters
CO2 is a product and creates gradient in opposite direction

CO2 moves outside to the atmosphere

2 Ventilation
muscles move in insects

mass movement of air in and out of trachea

how do insectsprevent waterloss
ton that is covered in a waterproof cuticles so
they hhaayeeawafigqiodooofte.ru

area where water is Lost through a small surface area

they inimisafiother
close spiracles when not breathing

why is water loss a problem

hey
EERIE
at the spiracle

ee
fun.ae
q

epidermis
 thegasexchange system in fish
fish use their many gills which give them a
verylargesurface area
the gills are highlyfolded and have many protrusions called gill lamellae and
kept supported and moist by water that is continually pumpedthrough the
mouth and over the gills

within the lamellae there are 2 efficienttransportsystems so they can

extract Oz 3times the rate of humans

concurrent f low countercurrent flow

water and blood flow through the water and blood flow through the
lamellae in same direction lamellae inopposite directions

water has more O2 than the blood blood reaches the end of lamella
Large concentration gradient lamella 80 Saturated with 02
but water at the beginning is 100010
Ozdiffuses into the blood saturated
Continues until water and blood Slightconcentration gradient
have equal concentration
Ozdiffuses into the blood
no more concentration gradient
qq

M
am

expose
l
how is the gasexchange system structured in plants

gasexchange occurs in the leaves which contain the following

waxycuticle
restricts waterevaporation and protects
leaveswithout blockinglight

upperepidermis
transparent with no chloroplasts

palisademesophyll

manychloroplasts to absorb lightefficiently

Spongey mesophyll

less likelyto gothroughphotosynthesis and covered in a thin layerof water

and allows better gas exchange

air spaces

allow gases to diffuse better

guard cells
controls the opening and closing of the stomata for gas diffusion

lowerepidermis

these protect the stomata

stomata
the site of gas exchange
 what is the role of the stomata
the stomata is a small hole which opens and closes to regulate transpiration
and allow gas exchange the guardcells control the opening and closing

Sto meathead J TFs

1 water flows into 1

cells byosmosis
guard
2 turgidityincreases so they
expand in size
3 inelasticinner wall causes
them to move awayfrom each 3 becomelessturgid and
other
4 Stomata opens
guardcells lose water
by actively taking in
potassium ions
2 take in ATP from
chloroplasts
move closer
4 Stomata closes

note during the day stomata stays open so plant has enough CO2

how is the Leaf adapted for the gas exchange

In summary
thin flat shape for short diffusion pathway and large surface area
many stomata
many air spaces
where doesgasexchange happen in humans

the main site ofexchange is within the alveoli in the lungs

how are the lungsstructured and specialised for their functions

trachea
an airwaysupportedbyrings of cartilage
to prevent it fromcollapsing

tracheal wall r
0
made ofmuscle lined with
i
cilliated epithelium which move
mucus down
a
gobletcells that produce mucus that p
traps dirt and bacteria a

bronchus
one of 2 divisions that lead to the lungs and lined like the trachea
they also have cartilage but its reduced as theyget smaller

bronchioles
themanybranches are lined with epithelial tissue that let themconstrict and
control flow of air

alveoli

tiny air sacs 300 µm

100 lined withepithelium and contain collagen
and elastic fibres which

allow alveoli to stretch when filled with air

Spring back when breathing out

site of gasexchange
 gasexchange in the alveoli

deoxygenated blood enters

less Oz in blood than the air thats breathed in

Ozdiffusion gradient
Ozenters the red blood cells
blood now low in CO2 and high in Oz

CO2diffusiongradient

Coz moves out of the red blood cells and into alveolus

how are the alveoli developed for their functionz

ik
largesurface area to volume ratio I
speeds up the rate ofexchange
a
I cell thick walls
of alveolus If f Ay
shorter diffusionpathway so also faster
capillary
Veryclose to capillaries that are also very thin

Shorter diffusionpathway

steepdiffusiongradient
allows diffusion to occur

ventilation
ensures the gradient is maintained

surface difference in
area concentration
diffusion
length ofdiffusion path
What is the mechanism of breathing

Inspiration expiration
breath in breath out

lungs fill with air lungs release air

Volume increases Volume decreases

lungs enlarged moves down and in

riubncg.ge
ribcage moves up and out revert size

pressure towers pressure increases

external intercostal contract

n act

gj
aDd_B

Why does pressure change

diaghramflattening and moving up

inoterenmalentexternal
intercostal muscles

pulmonaryventilation rate dm'min tidal volume dms x ventilationCmin

IItaataiFm.fmoEeeFeianiiungs breaths
ynolyumgsofogiif aedn jujube.io
how are the lungsprotected
the lungs are veryfragile and must be inside the body to prevent them
fromdrying out so are protected by
12 pairs of ribs which can be moved

mucus layers to trap pathogens and preventthemfromreachinglungs

many Cillia to move pathogens and particles

what is the danger of the lungs

theyincrease and decrease in size continuously

when increasing it could touch other organs
living tissue rub together
friction occurs and may cause tissue damage and kill cells

what are chemoreceptors

Chemoreceptors located in the
medulla

if CO2 levels in blood is too high

enzymes can beaffected
PH levels drop
impulses are sent to the inspiratory
part of centre
breathing rate increases
more 02 comes in
so coz leaves body
 hhaaeemmooggkoobbi.hn

What is haemoglobin

haemoglobin is a protien found in red blood cells and carries O2from the
lungs to the tissues in the body as well as Ht ions and CO2 to the lungs

what is thestructureofhaemoglobin
4 polypeptide chains which are
coiled into a helix

these arefurtherfolded into a

precise shape
all are linked together to be
spherical like
each chain has Fe haem group

each Fe combine with single oxygen

1 haemoglobin can
carry 4 02 molecules

how is haemoglobinspecialisedfor its function

It can changeit'sshape in the presence of certain substances like coz
in order to manipulate its affinity to oxygen and association

what is meant byoxygen affinity

this is howreadlyhaemoglobin can release oxygen

what is meant by associating dissociating

associating or loading is when

haemoglobincombines with Oxygen
and occurs in the lungs

dissociating or un loading is when

haemoglobin releases oxygen and
occurs in the tissues
 haemoglobin affinity

location 02 Conc 02 affinity coz conc results

gas
high 02 attaches
exchange
surface
high Low

respiring low low

tissue high 02 releases

why is 02affinity important

organisms in low 02 enviorment
I need haemoglobin with highaffinity to take in max 02
and high metabolism

highmetabolism organisms in normal enviorment

need haemoglobin with Low affinity to release more 02 to tissues

why do haemoglobin have different affinities

different amino acid sequence
differentshapes
affinity depends on the shape

so haemoglobin

Highaffinity
picks up Oz when its concentration is high and its harder to
release

Low affinity
releases Oz when it's concentration is low and its harder to
take in
 what is the dissociation curve
When exposed to oxygen partial pressure haemoglobindoesn't absorb
02evenly
e g low Oz concentration 7 1st Oz bound 7 results
4 polypeptide chains very 7
binding alters the easier to
tightly United shape of haemoglobin load 02

thfthgreat triphthong
 how does haemoglobin dissasociate

respiration occurs CO2

CO2 produced as byproduct in tissues
PH lowers CO2
I
PH affects haemoglobin shape 02L
0
now is low affinity haemoglobin CO2
Oz is released into tissue CO2

how does haemoglobin associate

CO2removedfrom tissues
low coz concentration
PH increases
PH affects haemoglobin shape
now is
highaffinity haemoglobin
harder to release 02 while transporting

what is the affect of CO2 concentration on association

Coz reducestheaffinity of haemoglobin so the higher the concentration

the more readily 02 is released

at body tissue at
lungs alveoli

high CO2 low CO2

rI
low affinity highaffinity
to the o graph to the
graphcompared
right
to normal
left compared
to normal
 Waarriication

what is variation

Variation describes the diversity in the genetic makeup ofspecies either through
the phenotype or genotype There are 2 Subsections called
Interspecific Variation variation within a species

Intraspecificvariation differences between members of the same species

what are the causes of genetic differences

mutations produce new forms of alleles chromosomes or genes which
may be
passed across generations

meiosis mixes genetic materials before passing to gametes

fusion of gametes as fertilisation is a random process

how does the enviormentinfluence variation

climate
soil conditions
these all play a role in how
diet
the organism genes are expressed
culture

PH
food availability
 what are the types of variation
1 discontinous variation

which have few distinctforms and no intermediatetypes

2 continous variation
which are not determined by a singlegene so enviormentalfactors have
an effect

how do we calculate mean and standard deviation

SD sun of C Value mean

or g x I
2

n 1
total of values I
how can we take a sample of a population
1 Random Sampling prevents bias 1 Chance

2 Use tape to divide study area into a grid of numbered lines

3 use random computer generated numbers to get coordinates
4 take sample at intersection of each pair of coordinates
5 determine population density

how do we minamise bias

large sample size

analyse the datacollected

 ANNA ggeenneesSaanndd

hhrroommoossoommeessWhatisDNA2

Deoxyribonucleic acid is made up

of
2 polynucleotide strands

nitrogenous bases which connect them

run anti parallel and form double helix
held by hydrogen bonds
complimentary bases

what is a nucleotide

this is the genetic material of cells and form

a chain via phosphodiester bonds

Note RNA and DNA have different nucleotides

DNA more stable and double

stranded

RNA more versatile and single

stranded to transfergeneticinfo
Why is DNA Stable
phosphodiester backboneprotectsreactive bases within double helix

Hydrogen bonding is verystrong

G C have 3h bonds so they make DNA stable

base stacking
How is DNA adapted for it's function
stable structure means limited mutations
molecule so carries a lot
verylarge of genetic information
double helix can seperate for replication
bases inside protected frombeingcorrupted orfromexternal physical forces

Complimentary bases allow for replication and information transfer

eukaryotic prokaryotic viruses

longer linear DNAstrands singlelarge circular Short DNA molecule

a

molecule
wound around histone Unpacked DNA
protien core supercoiling to be
compact prolien caspid
forms nucleosomes coat to protect the
Supercoiled DNA DNA
arranged as chromatin protiers RNA form a
fibres which loop to nucleoid a
double stranded
mane chromosome
no chromosome
Human have 46
How are chromosomes structured
1 Histones 27 Nucleosome

protiens rich in amino acids DNA wound 1.67 times

8 positive amino acid charges

ofthem form a nucleosome formstrongionic bonds with
DNA phosphate groups

enables tight packing

3 Chromatin fibres
nucleosome coils to form a long fibre
thesethen loop
4 Chromosome

µµ
2 chromatids
made
of
held together by centrosome centrosome

only visible at cell division

Usuallywidelydispersed chromatid
What are homologous chromosomes
Share the same structural features size centrosome position

same genes in same loci position

different alleles
must be separated in gametes to prevent doubling of chromosome number

what is a gene
Section of DNA located on locus which contains the codedinformation for
protien synthesis of a polypeptide and functional RNA

What is an allele

I'tenemasteafe.iouofgene
Mt

I
tapas
how is DNA replicated
1 DNA helicase opens up the double helix
by breaking hydrogen bonds
2 freenucleotides bond to available complimentary bases

3 DNA polymerase enzyme joins them togetherthrough phosphodiester

bases
4 antiparallel strand has Okazaki fragments due to ligase enzyme
5 each new strand has of original DNA

s 7

Why is it semi conservative

new strand contains of original and new
f
old strand becomes a template for complimentary strand
 prroottiieasyntthhes.is

What is the geneticcode

thegeneticcode is the sequenceofnucleotides in DNA whichcontaininformation
for protiensynthesis It is degenerate so amino acids can be coded by more
than 1 triplet Thetripletcanonlybe read in one directionalong DNA strand and
theyremadeup of 3 bases The code is non overlapping so each base is read
only once per triplet i 123456 is read as 123 456
the codeis universal so it codesfor the same amino acids in all organising which is
proofforevolution Thestartofeverycode is methionine but isremoved if not
part offinalproduct its then removed There are 3Stopcodons which mark end of
a sequence

howdoestranscriptionoccur ineukaryotic cells

1 enzymehelicase acts on specific area
of DNA causing the 2 Strands to seperate
and expose the nucleotide bases
2 nucleotide bases of template strand will
pair with complimentary RNA nucleotides
from a poolpresent in nucleus
3 enzyme RNA polymerase moves along
the strand to jointogetherforming a
pre mRNA molecule
4 Only 12 base pairs are exposed at any given time

5 Whenstop codon is reached it deataches and the pre mRNA is finished

base pairings are Ut A and Gt C

 Whymust we splice m RNA
Ineukaryoticcells the DNA of a genesequenceismadeupofsections called IntronsandExons
Theexon car codeforprotierswhileintronsprevent synthesisof polypeptides sosplicingremoves
theintronstocreate a functionalchain of exons and leave via a nuclear pore thenattach to
ribosomes and are readyfortranslation

1 e i e i e i e i e i e

D e e e e e e

I i r I i

3 extra chain
intron chain

howdoestranslationoccur ineukaryotic cells

1 a ribosomebecomes attached to a starting codon at one end of the m RNA

2 a t RNA molecule withcomplimentary anti codonsequencemoves to the ribosome and pairs

up with the codon on the m RNAThis t RNA carries an aminoacid methionine
3 codonand anti codonspair up each carryingamino acid

4 aminoacids on t RNA joinvia a peptidebondusingATP whichprovideenergy to attach

themtogether and onenzyme
5 the ribosomes movesto a 3rd codonlinkingtheaminoacidstogether in the m RNAsequence

G thisreleasesthefirst t RNAfromitsaminoacid and is free tocollectanotherfromthe pool

of aminoacids in the cell
7 processcontinues to buildpolypeptidechain untiltheyreach a stopcodon

6 thenribosome M RNA andlast t RNA molecule seperate andpolypeptide chain is done

7 triplets determincodons which determine the order of t RNAmolecules
 thestructureofprotiers
protienshave highmolecularweight and made upof amino acids which link
together via peptidebonds into a polypeptide chain Sometimes a singlepolypeptide
chain is a functionalprotier but we can link them togethertogether

primary structure
the sequence ofamino acids in a polypeptide
chain
this determines the number kind and
arrangement of amino acid forming protien
Carboxyl and amine groupformpeptide
bonds

secondary structure
the sequence of amino acids causes parts of the protienmolecule to bend into either
an alpha helix coil held byhydrogenbonds in the same direction as the coil

a beta helix which is a pleatedsheet in an S shapepatternalso held by H bonds

 tertiary structure
secondarystructure is bent and folded to form a precise 3Dshape which is held
by
hydrogenbonds polar 12 group polar 12group
disulphidebonds between R groupsof 2 aminoacids containingsulphur
ionic bonds positively charged 12 groups together
hydrophobic interactions amino acids point towards polypeptide

hydrophilic interactions amino acids point outward towards water

Quaternary structure
madeupofmultiplepolypeptidechains theyrefoldedinto a 3D structure and held
by the hydrogen ionic and disulphidebonds They maycontain a prostheticgroup
which is a non protier groupattached to protier
 the link between denaturing andprotierfolding
each protier has a uniqueshape

Charge in enviormertcausesprotierto lose 3Dstructure andturninto string of aninos

primarysequence not lost only structure

its now denatured and nonfunctional
note in rare cases we canreversethis byreturning to originalenviormentsince the
original sequence wasnt lost

what we chaperoneprotiers
Chaperone protiers are produced as they ensure polypeptide chains are folded in
the correctway

HSP 70 birds to hydrophobicregions of polypeptides to preventanyincorrectinteractions

from forming
HSP 60 Chaperoning are large cylindrical protiers with central compartment
polypeptide chain fits inside so its isolated from other pro tier molecules

Interaction ONLY between chaperone so protierfoldsproperly

found in endoplasmic reticulum

 fibrous protiers
made up of long twisted strandsof polypeptides they provide a structuralrole
and are
insoluble dueto highproportion of hydrophobic R groups in amino acids

Strong rigid
stable
e g Keratin i many di sulphidebonds so less flexible

collagen flexible 1 tear resistant

Elastin has elastic fibres so can stretch rewind stable flexible

Globular protiers
Made up of polypeptide chain that is folded into a sphericalshape and
providefunctional roles as theyre i
Water soluble hydrophilic R groups face outwards and vice versa
more sensitive to enviornert charge
irregular amino acid sequence
eg
Enzymes Haemoglobin insulin
 mmeeiioossiissaannddggeenneeki.ie warriatewm
what is meiosis
meiosisis a typeof cell divisionused in sexual reproduction involving 2 nuclear
divisions and producing 4 cells containing half the original amount of
geneticinformation

what are the stepsinvolved in meiosis

I meiosis one interphase 2 Meiosis two interphase
Phrophase Phrophase

metaphase metaphase
anaphase anaphase
telophase telophase
cytokinesis cytokinesis

what happens in interphase

the DNA in the cells is copied
2 identical full set of chromosomes

2 Centrosomes outside nucleus extend microtubles

what happens in prophase l

copiedchromosomecondenses into shape

pair up andundergo recombination
exchange bits of DNA
nucleusmembranedissolvesreleasing chromosomes
what happens in metaphase l

microtables extendacross cell between centrioles

chromosomes pair up at equator
centrioles are at opposite poles

meioticspindlefibres attach to one chromosome

what happens in anaphase l

meioticspindle pulls pair of chromosomesapart

chromosomes go to opposite poles
sister chromatids stay together

what happens in telophase l

Chromosomes are at opposite poles

full set are at each pole

membrane forms around them to create 2 nuclei

it pinches in the middle to seperate into daughter

cells

the 2 daughter cells each have 23 chromosome pairs one of them will be
used for the second phase which is the same
 what is recombination
Whenpieces of DNA are broken up and
recombined to produce new combinations
of alleles
what is crossing over
the point of the
crossing is called
the chiasma

partsofchromatids
genetic materials
are exchanged

what isindependent seggregation

Independent seggregation is the alignment of the 23 chromosome
pairs on the equator

they can go randomly on either side

this occurs during metaphase l

23
this means we can create 2 Combinations of a gamete
Chromosome mutations

a mutation can occur when chromatids are not split evenly during anaphase
and
may result in

Charge in number of individual chromosomes

may have 3 or more sets of chromosomes usually in plants

Chromatids may fail to seperate during meiosis so gametes have 1 more
or 1 less chromosome down's syndrome

normal
stiffens

Botafogo
 SSppeecciieess
aannddttaaxxoonnoommyy

what is a species

a species mustbe able to producefertile offspring and occupy the same ecological
niche

how do we name species

We use the binomial system i Genus Name species Name
1 capitalised Genus eg Humans
2 lowercase species Homo sapiens

how are speciesclassified

there are 2 main formsofclassification used
a natural classification artificialClassification

natural artificial
evolutionary relationship of ancestor not genetically releated
and organism
Shared observable features
groupedbased on shared features
analogous
heiarchy arrangement

advantages advantages
identifies traits based on groupings easy to develop
predicts characteristics shared by so
unlikely to change so stable
species

disadvantages disadvantages

highly mutable and changes as doesn't show evolutionary

new info is discovered relationships
usingtaxonomy
natural classification is based on homologous characteristics which have similar
evolutionary origins meaningthey're sorted into groupsusingsharedfeatures
we can use a hierarchy system made up of the taxons

domain Kingdom Phylum Class Order family genus species

Dear King Phillip Came Over From Great Spain
domain
eg for humans eukaryote
Kingdom animalia
Phylum Chordata
Class Mammalia
Order primates
family hominidae
genus Homo
species
sapiens

what are all the domain names what are all the Kingdom names

eukaryote animalia
bacteria Plantae
archaea fungi
protista
what is phylogeny

phylogeny is the process to find a species closest ancestor as all organisms

share the same unknown ancestor

all life share the same genetic

code in different sequences

the closer the branches the

closer the evolutionary relationship

tree can include extinct and

modern species
 bbiiooddiiweerssiittyywwiitthh.in aa commmmuunniittyy

what is biodiversity

biodiversity is the variety oforganisms in a given area or a measure of the range

of habitats
what is a habitat
A habitat refers to the range of physical biological and enviormental
factors in which a species can live in
what is species richness
this is a measure of the number ofdifferentspecies in a community
what is a community

A community is the interaction between a number ofspecies living in the same

area at the same time

how do we measure diversity

we use the equation

diversity total oforganisms of total oforganisms of I

ALL species ALL species
total of organisms of a
particularspecies
total of organisms of a
1
particularspecies

summarised into
eg d N N l
n n l
biodiversity is split up into 3forms
speciesdiversity ecosystemdiversity geneticdiversity

what is meant byspeciesdiversity

this is the number ofdifferentspecies represented in a community like having

100differentspeciesoffish in the same reef

what is meant by ecosystemdiversity

this is the diversity ofdifferentecosystems within an area so an area with

2 differentecosystems tundra grassland has more diversity than a forest

what is meant by genetic diversity

this is a measure of how many different alleles there are for each gene
in a population whichwe do by
comparing observable characteristics
comparing base sequence of DNA mRNA and amino acid sequence of the
protiers
often mutations are a primary source as theybring in new
alleles into a population
thefounder and bottleneckeffect

fewindividuals survive move location

bottleneck population
Carryonly small fractionof alleles oforiginal size decrease
population
founder few moving to
lowgeneticdiversity new region

diversityofspecies now restricted

what is selective breeding

Selective breeding is when humans breedmembers of a species with a desired
characteristics and get rid unwantedtraitsfrom a population and it is a form of
of
artificialselection

whatproblems can arise

reduced gene pool due to inbreeding

genetic diseases may be passed down unknowingly

can create physical problems fororganisms
loss of species variety
how do humans affectspeciesdiversity
1 exploitingagriculture

ecosystem controlled byhumans

selective breeding ofcrops so low geneticdiversity

competitiveness betweenspecies due tolimited biomass
reduces speciesdiversity

2 deforestation

forestshavemany habitats

land converted forhuman use

biodiversitydecreased

3 disrupt interaction networks

eliminatingkeystone species
impactsthose depending on them

4 pollution

degrades habitats

5 hunting
Can lead to extinction

7 Climate change
more natural disasters

icemelting floods

8 increased UV radiation
required practicalHel factorsinfluencingenzymme controlledreactions

1 Chooseindependent variable

temperature
PH
inhibitors
substrate concentration

2 which enzyme and substrate to use

enzyme substrate product

3 factors to consider

temperature water bath

PH acidic or alkaline solution

inhibitors must be enzyme specific

substrate concentration need a range to prevent saturation

 data collection
3 method
of
this will greatlydepend on the reaction occurring

4 Produce a graph
 rreequuiireeddpprraacctiic.cat HI22 i eeffffeeettooffssookuutteeiinnppllaannttoossmmooss.is

1 requires the following

boiling tubes
measuringcylinder
distilled water

Sugar solution
Scale

potato
ruler

2 Prepare to experiment by
a cut 6 or more equal Volumes
of potato
dry with paper towel
take note of their mass be equal

3 add 10cm
ofsugar solution

vary the concentration

by adding distilled water
so i

Om distilled water
0.2M 8cm distilled water
0 4M Gcm's distilled water

0 Gm 4cm distilled water

0 8M 2cm distilled water
1 Om pure sugar solution
4 Place 1 potato cube into each tube at the same time

5 leave for 12 24 hows

6 remove potatoes and dry with paper towel

7 measure their mass volume

8 Plot a graph
 rreequuiireeddppraacclliicco.at
tapping and deafpigment
33iicchhrroommaattoogg

1 require
leaf sample
filter paper
Chromatography solvent

pestile t mortar

pencil and ruler

capillary tube
acetone

2 cut section
of leaf andgrind it alongside 20 drops of acetone
I
acetone
Iy9
qqgg.gg
s.ggegp7 qgg
3 use pencil to draw line 1cm above bottom of filter
4 Use capillary tube to extract pigmentfrompestle and mortar and
blot on the line

5 Suspend paper in solvent liquiddoesnttouch pencil line

6 leave until pigmentsfinishseparating
7 Calculate Rf value

distance component travels

Rf value distance solvent travels

note compare
Rf value with known database toidentify pigment name
what can affect it
pigment affinity
lower affinity movesfurther

solubility
more soluble move faster andfurthest