PAPER BREAKDOWN.

Date: •95
. - 08 - 21

SURTECT CODE (9700)

PAPERS

Paper 1 Paper 4

Multiple Choice hour 15 minutes A Level Structured Questions 2 hours

40 marks 100 marks

40 multiple-choice questions Structured questions

Questions are based on the AS Level syllabus Questions are based on the A Level syllabus
content. content; knowledge of material from the AS

Externally assessed Level syllabus content will be required.

31% of the AS Level Externally assessed
15.5% of the A Level 38.5% of the A Level

Paper 2 Paper 5

AS Level Structured Planning, Analysis and

Questions hour 15 minutes Evaluation hour 15 minutes

60 marks 30 marks

Structured questions Questions are based on the practical skills of

Questions are based on the AS Level syllabus planning, analysis and evaluation.
content. The context of the questions may be outside
Externally assessed the syllabus content.
46% of the AS Level Externally assessed
23% of the A Level 11.5% of the A Level

Paper :

Advanced Practical Skills hours

40 marks

Practical work and structured questions

Questions are based on the practical skills

in the Practical assessment section o' the

syllabus.
The context of the questions may be outside
the syllabus content.
Externally assessed
23% of the AS Level

11.5% of the A Level

 H 80 Date: 28 -08 -
Gocfoce Akea to Yolume Rako i—

*
Tthe
Y.R
smalke a thing getsthemore 3.Ato

S:A y.R S.A

lem Y.R

No a Cbe with side 4Cm

S.A 6 cm S.A 4 6 q6 Cm *
Yo|. 1 Cm Yo 4 64 cm

S..A S.A 1. 5
y.0 .R

Cn
"m 10
-2e
B est
I0
m
Smtalle = Bigediide
m l0* oe SmaliesMiy
lo9
a

nm
Smalles

Magailicatien Jage
Actual
UNiTsmustbe the same.

Dooble Membrane Boond

pndia
Mhochon

2.Chloco ast
3. Nucleus
 Da

Mftochond a
Oganelle_ Ctuchaly fuacnally deint pact
Stalk hiot lickin _of a cell

U
Oer
Menbrane

Jme
MATRIx
M mbranc
C a
DNA
Cae
Ribosomes Eipids Jnter Mesmblane
0S
pc
Middle
Plasmodesma Lamela PuaN Cew

Vacuole
Go ai Boy

CełWal
Cytoplas
Ce Suface
Mitochondłion
Membrane
ob bosomes
Smoot
NocleaÉ
Eodoplasmc
Ret m Eovelop
N cltoluS, Rogh Endoplasnmic Reticlom
lchtonai
N CLEUS
 Date:_

NoCLEUS
을

*8
어에 0 이

do 이

39
 Date:_30- 08- 21
M HONDR N.

Baśic nîto Memlrane

Evesy menbrace is Supposed to be a phospholipid bi- laye.=

= 0 =

Outec Membrane Jnne Membtane = =

=
O

Circular DNA ests

el tepicafon.
RiboSomes *Drotei Synthesís - tochondiacan make Ihe o ▇
prot s.

Funchon o Mitochondion

v Aesbic Resphion C H 0 + GO, — 6Co, + 6H0

Glycolysis J r (Cytoplasm)
Reachion |Matx

Krebs Cycle (Matix

. Dxidative Phosphotylation(J ne Membane)
ETC (electton transport
chain

iesal eneigy Corcency

ATP
 Date

CHLoRoPLASr. Dute Membtane

nn
InnerMembraneh
fO

Stroma > Giran m

kibo9omes
Thyla od

Cirvtax
DNA Thylakod
Membtane

(sik of chlosphylt)
locahion Palisade Mesophy|l Ces
SpnayMesophyl Cells
CuvasdCells

PH rosy THEsis C, + ,0— C ▇ ▇ ▇

Lgr Dependrt Reocn

Thylaksid Membne

.
LgthJndependast Reochion
homa
 Date:_

CENTRIOLES

* A Dair near the nucleos Made up of 0. protein = TO2 UnN

location

Proto Flament

13 proto blameats

*
9 triplets makina cylindes

Functions:

1. Cel division organize spindle Atbess.

Important pact of Cytoskeleton
3. Act as transport routes proteins
PapER 3 Date: O・09 - 21

Merlfcolion Resolurion

MicRoSCoPEs

Elachen, Mltesepslioh Mecrsep

6EM TEM

At Ruer（os
Sinjeal Dawing
Plan Dagom Tee led Od
Qesokhion 」the obilly 2 dicelate beheen 2 points
* Mbre〈esoluhon Moredetail

Meotetien (o))(AOy)
Total Mae Lca Eyepid tcrveLens
agn
 Date: 04 - 04 - 21

Exchana Molecules between

E Cytoplasm a Nuclear Pores

mRNA
Huclers to Cytoplasm
Ribosomes

Proteins
Outer Nuclear Envelope 2. ATP Cytoplasm to Nucleos
IS RER 3 Hormones

Threads Chromatin
DNA Chemical DNA

Composition

Genes =
code. for single protein
Protein Synthesis Factory Analoqy

Raw Material Amino Acids 20

2. Production Ribosomes / RER

3. Packaging Gole Body
Vesicles

ENDOPLASMIC RETICULUM.

RER
flattened sacs CISTERNAL
RER is Continous with outer nuclear memblare

Mote layesed
Ribosomes outes
 Date:

SER

have SACS A CISTERNAE

FUNCTIONS

Rough Endoplasnic Refieolom Smooth Endoplasmic Reticulum

site
Loc pustio sypthesis producius of Rigids & steroids

transport Pathway for proteins Site ions in

muscle cels

GoLGA BoDy.

Flattened membranes enclosing hollow sacs

Called CISTERNAE

2. layesed appearance (not Connected)

Swellinas or end which ase

FUNCTIONS

Modification &. Pockaging Ploteins & lipids

Protein Non Protein

+
(Carbohy date)
Folding of Proteins
Removal 19 amino acids

2.
 Date:

L S0ZoME
Foond in Plant Anúmalcell
Single Memlo(ane u0d
otgo helle

Hyd olylic_enzyme
ptocuced by Go a Body

Dia Old
Dałhogeh K 1 Y

To ins
(. Dead Cell

R1a0s50

* Smallest
voanelle
2 p
80S (22 1 Malle(Sub -un
70S ( 7 m lasgelSub - it

80s e Eukoryoc Cellsa - Aatng olkarystes

Chlor p asts
Mftochondia
Chemícal Compstion
Proens + RNA foond on Qte Membtane oRER

RasM 0E META

Poes in a plant cell

Corhán stoads ytop asm

ea e

H,0 Aimno A ds TP
ucíe Minesals
JO a Hor
lot mone5
 Date

Ceu acuoLE

Lagef d pace(cell sap)

Conssts"
H,0 Nuhients
SucSose Minetal Sats

Pgoe e waste

Ceul wAw

Cellolose ibrs incres - Coss pattern

Non - 1ing
No - Elash Maîntaîns shoe
Freelypermeable Piei nhs cell om busling
Mddle lamella boundaf be u 2 cel walls (adiacen)

Plant Celolose
Bacleha =
Fu
" q
Peokdogloean
(hi

f ARYoTIe Ceus PaosRyone Ceuse

(10 - 100 m dianeter Smal|l (typically0.5- 3 uum
Looe
n

diamete o 000 Vb. uka o es

T e ucles- nuclea( envelope No hve uc▇

 Data

Yiros.
Acellular
Nocleic AcidONA / RNA
Doou Covetog* Paten Cat (Coso)
On (eplicôte nsidde ho st

Nochatactel lics livog

Smalle than bactea
rganisms

FLAGELLA
Bołh aseiny háx/ whip She shwctves (inmony Gukatyotíc)
Cia Smaller in Size manyinnumber

agella e kess tn teerber but latge

Structvre of Clia an
( +2V Cell Suroce Memorane

Colum
mcrolvbules

2 Central mitotvbule
Ang o micohbole BasalBody
p (s

n0) 1 mcrotubule paút (MTDs) Doublets

a ylindero
Coepl i t re iag Jncomplete ( q mictolubule

of 13 o proło(slameat tiptets
proteftlameats
10
| q + 0

w afms that Rroten

Amicrotuulehas Oyne
 Date: 5-0 ▇
B L GC MouCUES
Mactomolecu e
a lagebilngical moecele Such asa praln
olysachańde o( ucl acid

Monomers Singlevnits same e Shape

No
Monome 5
1on sacchaide
oyme.
Plvo echarides
Polymeázathion

Amino Acds Prołei s

*Wałke(sa olarmolecule .

C EMICABo DS
Jonic
shaieg s eual
Complehe hiansle
Covalent — Shadng
Metallic

H,0
unegualsharing
Mol . Jorormula

Str cturalFormula. r ueh

8 o y s tends to take more

shae

t has a negative pol

+

6
H
H
hydogens hauč"
sive pole
( p le)
Polar Molecules
HydioBond
d
 Date:

WHAT IS A POLAR MoLEcULE

A that has attraction between

dipoles resulting in

molecules

Contain the elements : H &

2: 05 in

Genesal Formula C. (H, O),

3 Categories
Monosacchalde
Consisting
siogle Sogas unit with the
general formula (CH, 0),

2. Disacchaide
molecule Consisting two monosaccharides

joined tog ether by glycosidic bond

Polysacchaide
polymes whose subunits are monosaccharides

joined togethes by dyeosidie bonds.

Monomers are Sugars

Classified according to
of Carbon atoms

2.
 려

GwcosEz
Glocose is a hexose
tseae malue ome품 CHa
Maj r Source of 9yi espratien in test Cells
taea
Basic Res loiy Subshake
olymes.

Gwcos SrucIU AL FoRM LA

glvcose glose
CH0H
CH,OHa
H

4
C
O

OHz 아H
OH OH
OH

z
J the
OH g p o0Carbon
gocose
piouels beo the ing
* J glueose the OHz
goup of Carbof atom 0

poieels * above thC

n9
 Date:;

DıSACCHARIDEs
Malłose 2x - glocose
Suctose - glucose - dvctose
lacto6e (Al goillas ase mode black

H DrOLYS1
H 0
Dimes
MonomeS
CoNDEMSAmoHREaC ON.
H,0
MonomeS Dimers
CH,OH

( C.

D 0H

H,

monosacchade +monosacchade - disacchafdet

 Date: 20 -09 - 21
MorOMER
Relatívelysimple molecole
Basic buildina block orthe synthesís of polymets
Many monomers Comne to loim polym ess', uswally
ia Condensafon reachons

e.g
MonoSacchaides Amino Acds Nucleotídes .

Po yME8
Giant Molecule

Compsed stailar sepeting u fis joned kogciher

e
Polysacchadides Ptotns Nuclei Acd

Redog g Glucose Fuctose Maltose

Nlon - Reduct Sogois : oesse

Mnemonic Go redvcton dung execse s0
WIU
Do (ege

PoL SACCHARDE
PolymeS Contai inmany Monosaccharideslinked by olycosidic
dormedE Condensahíon feacns bonds,
by oo06 mononeis à 5 gcosidic bonds
e no of bonds Monomes - 1

Molinly sed ason esetoz store and as struchutal Componenls

of .

C-
Stach Cellolose i plants

G Coge i an mals
 Date:

Starch
Made
Op of 2 substances

Amylose ( Milo - lose Packer)

Made by Condensation between Xx- glucose molecules

Chain several 1000 1.4 linked glucose molecules
Glycosidic bond Dehveen Carbon 1 Carbon 4
Chains ace Curved 100
Chains coil up into helical shuctores
Chains

b. Amylopedin ( Milo - Tin)

Made by Condensation between a - glucose molecules

with 1.4 linked glucose molecules
Chains are shorter than amylose
Chains are branched & blanches are
formed by 1,6
linkages

2.
Glycogen
Made molecules
linted togethes by
aycosidic bonds (1,4 ¢ 1,6 linkages

Glycogen molecules are more bronched than

amylopectin

Therelote, it has an increased fare

hydrolysis
 Date:_

Cellulose

Most abundant
ofqonic molecule

Mechanically stone Hiah Tensile Strength

glucose
Successive B jucose molecules are linked at 180 to one another
in B
glucose the OH on Carbon 1 projects above
the ting the Successive B- glucose molecle has its OH

Carbon 4 below the

on
ting

Freely permeable (tbres

60 70 molecules

Many microtbils combine to

sim/ cellulose bres
these form pattern

LIPIDS

molecules Josoloble in water

Acids + Alcohol (ex Glycesol =

Esters (Lipids)

Contain C,H,O with higher

Plopoction of H
lower Proportion
 Date:

tatty Acids

Unsaturated

IWo Types
OH
Acid
Head a. Monounsaturated

/EMM 1 Double Bond

H

Tai o Polyunsaturated
H H A-A-^ 2 of moce Double Bonds
H H
H
Double Bond
causes Kink 2. Saturated
in tail
H H
Straight hydrocarbon toil
C H with ho double bonds
11

H - H

Alcohols

Diganic molecoles Containing hydoky! groups (OH) attached

to carbon

Condensation Reaction
Fatty Acids + Alcohols Esters +

HO - CoO C- H,O

Carbon pic atoop o acd reacts with

hydroxy groop of alcohol
to
form an ESTER band
 Date:_

PROTEIN:

A diverse and Complex polymes molecules

made
long "chains of amino acids

Wide
Rage. $ Biological Roles
Structural
body tissues, eg moscle
moin Component skin etc

Catalytic al enzymes ore proteins reactions

many hormones & receptors ase proteins

Immunological : all are proteins

Amioo Acids
hove

each
the

one is
same

the
genera
nature the R
the only
difference between
de ines on omino acid

Central Carbon
Amino Group H Carboxylic Group
Acid

Side Chain

OH-
 Dat

Bolymeisahon of Amino Acids

Amino Ad Amno Acd CoNDEson
R H,0

H0 4 H 0H
H
Ppde Bond

Dipeplde
OH
a.ka * Amide Bond

Polypedes
When mor amino acdse are odded to a di phde
Poypep de chan s dotmed
*A ptoteinCo sísts o mote pelypepidechains folded
oło higblyspch 3D shape

4 le ls o Shuochte in a Prohein
imaty1 era(y
Te

. Secondacy . va r t e s n a c y
 Date:

Number

chain
and the amino acid seqpence 012
Only peptide bond is Dresent

Secondary Shtocture

A
polypeptide chain coils into Known as apha
Helix This is a secondary stucure

a result
o polas characteristics)
between co- and the

amino acid
Jous places sheod Bf it.

Sometimes this hydrogen bonding resuts in B- pleated sheets

much looser & straighter than Helix

Tertiary Shrocture

protein molecule resulting com

the 3 dimensional Coiling already folded ( doe to X-Helix E
B pleated Sheets chaing amino

CO - groups

2. Disolide Bonds form between Cysteine molecules They ate

covalent bonds Broken

by reducing
 Date:

3 Jonic bonds fom between fonised amine

carboxylic acid COO g(oops

Bloken by ph chang

4. Weak Hydrophobic Interactions occur between non - Dolar

R groups Although the interactions are weak the
are cepelled
g Coups tend to stay together Decause they
by the watery envifonment around them

lt is a spheical and
founded arrangement of 2 of more
polypeptides . of of polypeptide or
non protein
Component Such as Haem, in protein molecule.

Protein Containing ison A Quaternary Protein

Ho +40.

ty Collies 02

26 Polypeptide chains
Canter
(p - 0050)

Hydlophobie Outer

Each Haem group attaches Oxygen molecule to

Wheel
molecules of atoms attached to
 Date:

Types of Roteins (based on solobsitty

Globular
Hydrophilic pottion on outside All

enzymes are
globular proteins
b. Insoluble + plas important roles in stroctoce

e.g: Keratin collagen

Collagen
Composed helical shaped chain
+ every
amino acid is Glycine

Alanine

above
helicals wind together to form collagen
molecule

Note
glycine is the simplest Amino Acd chains Can

be very tightly backed

Many o the tiple helices lie side by side linked ho

each other by Covalent links

Connected at
staggered ends"
Greates Strength
PRACTICAL. Date:

What is an expeiment 2
Effect of tempesature on enzyme action.
Enzyme Action

Directy Measured
i.e. No. of Bubbles Produced

* Independant Vaiable

Skil
Manslating inlormation from text to to tabulation

(tables)
Controlled Yatable
Time

Spe o Enzyme Volume A conc. enzyme

Control makes experiment valid

your
Repeating You! experiment makes it reliable

* Interval of independent Yariable most be equally spaced

Concentration
Volume
 Date:

Proportional Dilution

Stock M,Y,
31.
Solution (4 )(z) : (3)(10)
7:5 cm 3
10 cm' 9.5cm® water
* We will use Stock Solution every
time to make dilution.

Serial Dilution

* We do nor
go back to
the stock solution for every new dilution.
UNIT 3 : ENzyMES Date: 18 - 1O |

Eazyme

Cloblar Rrokins
Hydtophilic
a. Sphe cal
b. Terhaty Skrovcture Hydłtophoic
C. Hydrophilic Gtoups Polar
dWatec Soluble

Bielojiea Callye
They catalysmetabolic eachions
Catabolic Anabolic (Bankdoan Bild -p)
Speeda o S do

A+ 8 ooiom
+D

D No alle
eg ilib m beh en eacłonts▇
n Concenhratíon + Nochemically used p ina
Chemicalreaction + Can be Sed

Jnkcacel lar enzymes that Całalyse 1ea chons

w hinCells.

Exhtacellular: zymesthaCtlyseteacHens
outside cells + secreted by Ces.
 Date:

Lowers (EA
the
Activation Enesay

Substrate

Products D

Rogtiess of Reaction
A Axis labelling Enesqy level of Products
Axis labelling level of Substrates
Graph line stairs com Substrate
D Graph terminates +
End of reaction
E EA

How does the enzyme lower EA

1. Provide on alternate pathway for 0. chemical reaction

2. Enzyme brings reactants close together

Enzyme Substrate Complex forms quicker
4. Puts stain on so that bonds ae bloken
formed easily

Lock & KEY HYPOTHESS

MECHANISM OF ENZYMES

THE JHDUCED FiT MODEL

 Date:

locK Key
A mechonis ofenzyme achonthat demonshrates
hos the ubshahe iis fntothe enzyme jist
ke Hhelock key
Col1sion

Enzyme SobsttateCome close

hogeether.
*ctive Collion (Kinetie Enegy)
( 1le▇

Shce the hape of the ubshsahe

isComplimentary the acive Enzyme - Sosttate
Ske the enzymean Comp
lechiv Colliesdlts in the (ESC)
Jeimalon ESC

Tempuoy _Boadeormed behoeen acheste enzyme

Hydegan Bods
Tis ellectiely oes the E

nzymt Ptodct Comp e

Reachíonalmost Complete
Poducts ottel ased

Poducts(eleosed (om aclive te

Enzyme Resed
 Date:

INDUCED FIT MODEL

Shape substrate is
not exactly Complimentary
Active site
of the
enzyme Changes shape slightly

Substrate Changes shape X Incorrect

Too General

This results in BETTER FiT

The active ate a subshate are now complimentary
The active the resumes its normal shape

on
Enzyme Action

Re a c t i o n
20 30 40 60

temperature

As the tempestore increases so does the rate

reaction

Temp. Effective Collisions Product formed Rate

minute
pes ont time

Optimom Tempesature lom over rate is maximum

( enzyme working @is best)

D Denaturation storts €
Complete Denaturation
 Date:

Effect of pH of Enzyme Action

Hydrogen ions Can with the R

acids
by Lecting fonisation of + ie
chases,

This affects the ionic bonding which io

the 3-
dimensional arrangement the

enzyme molecule

of Substrate Concentration of Enzyme Action.

* Negates Poportionality
As Substate Conct - R.o.Rt
High @ Start
Best past to calculate then starts to decsease
tate Finally Ro.R reaches a plateau (
Substrate Concentration
man. voloe mak

Theorefical maximum fare (velocity of 0. reaction

an
enzyme catalyzes
C Ymar all enzyme molecules are. bound to

Substrate molecules

Michoelis - Menten Constant ( Kn)

Exam Perspective
•. Deline How to determine
rom graph 2
Conceptual
Calcolate Valoe
houd to that valve
get
 Date:

Ho to determine Km9
Take Yatar

e 0
econcle Yaue

Sobshrate Conc. on X-axis.

K pesats a suieof alli by ▇

mol |dm Zyme 1of tsSobshrate"

TKe "Ay Ke . TAfa

Conseg ences Conse ences
less el ective collisfons More el echve collisíons
Such enzymes form ee Such e z jMm mole ESComplexe
sComplexes (Achive site (Achive iteo ▇ enzymesa s e a
Such szymesaue less g ▇ betke ubshrate)
fo sobstrate heachon akes less Kime to teach
Re longe
(each
nat
Hgher Conc.,
*lLessConC. sabshate ed
Subshrate to (each
ied
UNIT - 3 Date: 08-II - 2
JN IBI T RS

Competitive Jnhibitor 2. Non - Compehtive Jnhibitor

An enzyme has anachhe síte esother than the aclive

site calledallosteńíc sike

Non - Compe hhive Jnhibito Compelition blo Subshtote inhibiło(

bedsto alloseic ik Cawuse chonge in the stuchr

the achive site

Ache s e is to longes Comptimenhany

R.0R i isirreyersble

Compehtive nhibitorhitibl wbstate Comete b Bind eneyne

CAsE A C: Conc. Compehitive inhibsiło binds to

Sub.Conc achive site

CAse B C Conc Gobstroke binds to the acive

Sob. Conc sie

. Ym Y
* Reverble Ellect ed Comp. Ihi ihr on , K

0 Km valve Km
ntt
(al:iniy—
RoR
h6iłod
Yma *= Same

K Subshtołe Conc
 Date:

remaing the same because at high substrate concentration

the leaves the active site & the reaction progresses
normally remains some & Ymax is the same

Effect of mCg

IMMOBILIZATION OF ENZYME

Lactose LACTASE Glucose E Galachose

UNIT 4 ME B ANES Date:

a. Funchonsof Membanes

Forms a batier betweenthe Cytoplasm ex t ro a l e n i o m e s t

ese issue (aid
pakacts the " oeganeles dim danoge _pierts he_ coly
o palhoen
Cell Sonace Membianes play a signl icant (ole incel

snli
becavse
has ecephe o ge zigoaling
which Couldbe a hofmone of

nerohransaHte

adso cell sodace colicen by doing cell ecoibon

5.Plays a (ole in cell-to -cellodtheson -—

A site doc enzymes Cablyzing cions

7. anchorsthe cyłoskeleton .
Conhos enhy exll e sobstoaces
8. Celmembrone selects Substances that enter o lea e a Ce1l

eme bdegn bood with wles e dhbility

HhuS is esponsb
oor the biliły phagocytsis,
 Date:

b.
Components ef Membranes

Phospholipids

Hydrophilic Head
Hydrophobic Tails
attracts water repels water

BILATER

Hydrophilic polar phosphate head

Hydrophobic of Don - polor acid tails the hydrophobic

Fatty acid tails may be of unsaturated

Polar
head Jorms hydioggn bonds with water

Polar head also Stabilizes the membrane

Unsaturatedl catty acd tails Contibute

b Juiditly o the

membrane

These hydtophotic tails are a

polar substances lons into or out Cells

Phospholipid molecules
Water
with heads

* Hydlophobic Cote
When mixed with water phospholipid molecules arrange
themselves into blayer: in which the hydrophobic
tails ase attracted to each other
 Date:

* When exposed to water phospholipids dotin one

two stroctores

Spherica

lakes on a number shapes

CELL SURFACE MEMBRANE

branching carbohydrate branching carbohydrate attached

attached to a protein to to a lipid to form a glycolipld
form a glycoprotein
hydrophilic head
transport protein (channel or carrier
protein) has hydrophilic interior for
ions and hydrophilic molecules
hydrophobic tails

outer surface

phospholipid

inner surface

one phospho-
lipid molecule cholesterol proteins
in both layers

Copyright ZEESHAN KHALID

Thickness: 7nm

* Freely Permeable NoT X Filly Permeablex

 Date:

Fl idMoic Model

Fud : Phopholipd prohein molecolesmove abou (dilos

wihi theímonolay.
atten
Mosaic Dierenk hpes rołeimoleculesscattered

Componenłs Fl idMosaic Model

C LESIER
Słahilizes membfane
y oido chanical słabilily
Leddles the Ahidily o
menbrane byprev nting lateral
mo emenh phóspholipids,
Has a hydophilic heod a hydophobic hil pr▇
ossage of ions polatmolecoles thccah membane

Inhtinic Płote i s
PRoTEINS Gtliośic oleins

a. Intínsíc span entire bi- layer

Rotein ((han
Channel : pned shape wohes flled poie U 0
0
ne channel hycliophilic
Outer channel hydophobic C0000d

Canier: - Con change i shape cafameointa daoge

o000 cc0co

Eazyme 0
Cotier oteio
p

Gycopołein
 Date:

Glycoproteins Receptors
2. Cell Adhesion
3.
Cell Signalling

b. Extrinsic

Cell

LIGAND

A figoal molecule (e.g. Mormone at the cell

membrane.

Binds with a spectic receptor. then may may not he

cell
in by the

attached to the protein receptor

3. moves
Lay ftcom
it to activate an
enzyme.

Thic enzyme releases 0 molecule called a

second messenger
Which i9 Small + soluble it
dilluses thiough the cell

greatly ampil ing the Signal

5. This initiates
sigalin cascade with amplification at lach

Response Secretion

Movement

Metabolic Change.
UNIT 4 Date: 20 - I - 2

Movemat into ot Cels.

Dilfosion
Passive Pocess
Toe poces ccc for amall molecoes acio9s the membo
Dean the cont. giadet.
Phospholipidsin the
bi-laye Move withinhesent (esulking in short-

lived potes bogh wlichanall mobecles Con_ ps thuug

smosis ( )
Wates Potential Pokenlial o H,0
Piesence of utelo(s wałér potenhal
Net Movement o Wakes Molecules
ncipient plasntolyss i the instonce d detachent of cell membiane.
bejo plasmolyss,

Active Tansprtt
Achiye Proces
Re es ATP
ee ou Guad en
Ue memloíone Haneport piohein (Cotier Rokein
Merbiane heanspr pottin specilic to the molecae tansported

Facilałated Di sion
Ooson Happenig thouah aty membtane Pioten
 Date:

BULK MOVEMENT

Vesicles moves towards cell solac membrane

of vesicle with membrane

Contents secreted / released

Active Pocess ATP)

b.

Attachment of bacteria to receptors

ability to atach to antibody ( bound to antisen on bacteriom

Bololding af membrane pseudopodia

UNI 5 M oTic Ceu CyceE Date:. 27 -I| - 2

Chtomoomes |Hskone)
Chemical Compohion — DNA Pioteins

Chtomafi *DNA + Protén

chromak loosely coled

Hetechtomaln
s'
HighHly coiled
Numbeo chcOmdsonmes s fed per pecles=
Humans 4 23 pis
Sonflow 34

Occu in pie = homdogoos Chomosomes

Chtomo%omes
es8 olicahion : DNaReolcation

1 DNA molecole 1 chromosome

chtomMo9me DrA Reolication 9 ste chtomatid

ds

1 Chtomahd Cenho ere. 2 DNAmolec les

Connecs ster
chíomatid

ONA Replicationoccus ineide the (udes

 e.

Cew DiviSION.
Mitofs Mesís
h Posent Cell
Pa eot Ce
Dpl id

2n
o
,0 o,0
Dau Dav hte(
agtite C ell

Cel Cycle a seece d eertsthattakes place Lcomone

Cel|diísion vn’ the next .—

Gutoth
3 PHAsEs A) r RPe syuthesis
2 Grolh
(B) M 1TosIs

Ropna Metaphase Anaphose

Telophase

C) tokines

C2

Jntephase
piokóns

RNA
-Call giaalh
*A ytheas
Enzyim
SCyłtokeneis
D anelles
MIToTC Ce C Le Date: 29 - II - 2

a. JNTERPHASE
G1 : 2. S
Rotens DNA Replicahion Synthesis
RNA

Eozyme 3. C2:
Oi anelles Shorte phase

CellGt Pokéns Ke micsohuboles ase mMade

b. MI 5S

Rophase Hetecochiomal
Chromosomes Condense isíble

Nuclea( envlope disihheguh

Nocleolus aso disnteotaFes
Cetíoles (eplicoke move toadee
Po S
Spndiee bS (Made 1om Ast Certe
A pair e centioles
ptote mohubu es)beginin to In 2nd Centfole
bu Cenhrosomes.

Mekaphase:
Ceorosome (each opppsite po es spndle

Sn e anond oy ma wmes
Spindle bess attach to cenhrometes.
Spindie ibesspfically attoch to theKinehochoies, on the
Ceoktomee
 Date:

Anaphase
Spindle bers shotten € pull at the

Centromere

The Chromatids start to be pulled apart by micotbules &

move
opposite oles

spindle fibers (micctubules)

are

The chromosomes reach the poles

ou? the spindle.
The spindle ibers bleak down

The & it reassembles

nuclear envelope reoms ftom vesicles
around daughtes chiomosom

Chromosomes (Euchtomatin

CYTOKINESIS

Divison of Cytoplasm

Cell
Plant Cell Development 0. cell plate
 Date: O4 12 21

CANCER
> Cell Cycle is controlled process

Errors
checked by oncogenes (tomor suppressor gene)
* ase

Uncontrolled Division Mutagens cause mutations

Carcinogens cause

Uncontrolled Mitosis
No death

No contact inhibition

Mass of cell is formed

benig Tomor To cot epfead

Spread

Tomor cells invade other tissues Secondary cancers

Loren thoughoot the body.

STEM CEuS relatively umspe cialized cell that retains ability to

an onlimited
nomibes of times

Potential New

Sperm Cell Cell

Organism
+

20

Ability to divide
cell
 Date:_

cell
Totipotency ability to dwide into any type af specialized

Stem Cells Stem cells

Embryonic

Multiporent
iro
Adult stem cells only able to
specialize
cell
types
BONE MARROW = Only Blood Cells

TELOMERE

Evestime when chomosomes are epicated pott of the

Chromosome is NOT copied

*
prevent the loss important genes TELOMERES

resent on the ends chromosomes l

> Telomeres Contain Don - Codling genes

de Consists of a (egion non.

Codina tepeated bace sequences
preventing Joes thes

Doing DNA replication the enzyme that copies the

ONA Continue all the way to the end o ONA
molecule
each time cell divides the ends of ohiomosomes

becomes shorter
This results in a loss
genes
par-
Thos to Prevent this felomeses ate used instead

allowing the cels h divide without

losing genes

1
DNA G PROTEIN SYNTHESIS
Deoxyribonucleic Acid
DNA Molecule
☐ DNA molecule
contains
information
determines inherited
that

characteristics .

'
Base
Nitrogenous
<

Nucleotide phosphate Group

P N

Pentose
S >
Sugar

<
DNA
DNA Nucleotide Phosphate Group P Nucleotide N
Deoxyribonucleic Acid

Deoxyribose Sugar ,
S
Pentose is not
preferred -

Base Adenine
Nitrogenous :

Thymine
÷
: 4
Different types
* Basic unit
of DNA molecule
1-
Guanine of
nucleotides
Cytosine .
DNA

ATP Adenine Adenosine Triphosphate

Ribose P P P
 phosphate RNA
RNA Nucleotide Base Adenine
p Nucleotide N
>

Nitrogenous :

Ribonucleic Acid
Thymine
Guanine
s
Ribose Uracil
>

Bases Bases that 2 types

Nitrogenous 5 split into :

PURINES PYRIMIDINES
° Adenine °
Thymine o Uracil
°
Guanine o
Cytosine

Double
ring Single ring
° °

> >
Heavier
Lighter
° °

DNA : A. T G. C
,
RIYA : A ,U ,
G. C

* Bases
follow a
principle of complimentality .

A with T G with C
A T G : : : :C
> Hydrogen Bonding
 -

Bases
Nitrogenous
-

Sugar
TF5E
a-
Backbone
.

'
Uncoil '

3 5

* Two antiparallel strands twist in

phosphate
opposite directions to
form a DNA >
Sugar
double helix .
Backbone

Nitrogenous Base
pairs ' '

5 3

1 DNA strand A polynucleartide chain

Uncoiled Double Helix S
DNA phosphate sugar Backbone

P A : : :: T P

s
S

P G C p

s S

P T : :: : A P
K

S
Phosphodiester
Bond
covalent Bond

Hydrogen Bonds
<
DNA Replication
DNA Replication
i. DNA double helix unwinds on coils to
form two
strands
single .

The DNA
2 .

enzyme
Helicase breaks
Hydrogen
Bonds between the base
complimentary pairs on

DNA strands
the two
poly nucleotide

used
3 .
Both
of the exposed original strands are as

templates .

4.
Complimentary base
pairing means that
free activated
DNA nucleotides added to their base
are pair -

A with T and G with C .

Condensation
5. reaction
joins nucleotides
of the new

strands DNA catalyst

together using polymerase as a .

And this polymerization reaction results in the

formation of the new

Polynucleotide chain .

This is that continues

6 .
a
step-by-step process
along
the whole
length of DNA molecule .
DNA Replication
7. Initial
unwinding of DNA Double helix forms two

fork like structures known as Replication forks ,

known bubble
collectively as replication .

8. Replication is semi -

conservative which means each

newly formed strand

DNA molecule contains one

from the original DNA molecule and one

newly
synthesized strand .

9 .
DNA
polymerase is also involved at the end
of
replication in some
proof reading and repair .
Meselson and Stahl Experiment
1
Follow the Numbers for I.
Isotopes Nk Mis
the Experiment supplied with His and
left
2. DNA ☐
Nitrogen to divide
L

§
✓

p µ
Bacteria IN / His
•
* Divide until all Bacteria had
S

2 N15

3. Bacteria DNA
§ § >

4 .

Centrifugation Nia N1S

Nia
3
To determine
if all bacteria Allowed to
•

had His Bacteria "iNI His replicate once

¥¥§#
N14
"" -

His
His -

His
Allowed to replicate

#
"" more . N14 -

4 His -
Protein Synthesis
i.
Transcription 2. Translation

20 Amino Acids , triplet Codes

eg . GGT Glycine

Transcription Results in the

formation of mRNA
on DNA
mRNA Messenger * The triplet code is
RNA rRNA Ribosomal
degenerate .

RNA
tRNA Transfer codons -

on
Protein Synthesis
tRNA i. Clover shaped 3 .

Hydrogen
bonds in some areas

stranded RNA nucleotides

2.
Single 4 .

5. Anticodon
types of
6 .
20 amino acids > 20 tRNA

7.
Specificity of Anticodon =

Type of Amino Acid

Translation
Mutations
Addition Deletion
.

Substitution

SICKLE CELL ANAEMIA

CTT

Yal His t.eu Thr Pro Glu Glu Lys

Yal His Leo Thr Pro Tal Glu Lys

CAT

* This substation occurs in one

of the P globin in

haemoglobin .

DELETION
TAG TAG TAG TAG TAG
✗

TAG TAG TGT AGT AG

Frameshift : A
type of gene
mutation caused
by insertion
or deletion
of one or more nucleotides

resulting in incorrect
readingcode
of theduesequence
of triplets in the genetic to a

shift in the reading frame .

Transport in Plants
Assimilates ? Levels
of Organisation How?
substances that will
Why?
become incorporated into 1 Cells Transport in Plants
biological tissue .

Tissues What?
2

3
Organs Key Words
nutrients
"
source : source
of assimilates .

u
Organ systems sink : where assimilates are
required .

Mass Flow :

flow of water with assimilates

s
Organism due to cohesion .

Cross-Section of a Stem
"""ar Bundle
-
-

cambium ÷ "
'

-
Epidermis
"

Cortex
"

Fibre
parenchyma
Phloem Xylem
PLAN DIAGRAM
Transport in Plants
Root Hair Cell

*
Responsible for 1-10 absorption
of
'

rate endosmosis
5. A to Volume Ratio Quick
* >
Absorption
WATER
of

Cross-Section of a Root
> Epidermis
cortex ✓
r
Phloem
Endodermis ←-
Xylem

Pericyde
Transport in Plants
Parenchyma (Packaging Cells)
•

Thin walled cells .

Used tissue
as a
packaging
-

Metabolically very
active
.

Can be used
for storage of starch .

Support .

Prevent P.M
wilting cells
.

In leaves contain chloroplast

sp.NL cells

Parenchyma forms the cortex in the roots and stems

-

Collenchyma
•

-
Modified form of parenchyma
Extra Cellulose Cell Walls >
.

Thicker
-

Extra strength .

leaf Mid Rib Collen

Chyna
"
> >

Sclerenchyma
•

Non -

functional xylem .

+ Functions to give extra mechanical support .

 Phloem Structure,

Transport in Plants Loading &

Unloading

Phloem Structure
Phloem is tissue
a
comprising
> :

i.
Companion cells
2. Sieve Tube Element Technically not a cell

>
Align on top of one another to
form sieve tubes .

> Sieve
to
plates with sieve
pores at ends
of tube element
support them
Plasmodesmata
3 .
connect 14 2
allowing cytoplasm
to be shared
for loading &
unloading .
Transport in Plants
Loading and
Unloading

Loading:
i. This is an active process that
requires the use
of ATP

from mitochondria in cell

'

companion .

2. Ht ions are pimped out

of the companion cell
into the cell wall b/w
companion and leaf cell
source
using a membrane
protein .

Ht ions concentration in cell wall increases

causing
3.
+
back into the
H to move companion cell together ,

with sucrose
through a
special membrane protein
called Cotransporter Protein .

> As it allows Ht to

facilitated diffusion pass only w/ sucrose

4. Sucrose
diffuses from companion cell into the

phloem tube element

through the plasmodesmata .
Transport in Plants Mass Flow

Mass Flow:
I .
The assimilates are inside the sieve tube elements ,

its lowered it has

causing potential
water to be a

more
negative water potential .

2. Water thus enters the sieve tube element via

osmosis
from neighbouring tissues
,
including xylem .

3 .
This causes an increase in the volume
of water
in the sieve tube element in increased
leads resulting
an
,

Water Potential .
This to increase
an in
'
the
hydrostatic pressure !
and
4 .
Since at the sink
unloading occurs

sucrose leaves the sieve tube element

, hydrostatic
pressure ✓ .
This produces a
Hydrostatic Pressure
Gradient
giving rise to Mass
flow .

Cohesion is as a result
of water molecules
being hydrophilic .
Transport in Plants Xerophytes

Xerophytes: Desert Plants

*
Adapted to survive under scarcity of water .

> Inside
surface of leaf iswhich
covered by hair like -

structures Trichomes
- moist
-

trap air ,
reducing
the water potential gradient ,
decreasing rate
of
transpiration

>
Have sunken stomata which too trap moist air ;

stomata are absent on the outer

surface of leaf .

lower epidermis

i. Tick
waxy cuticle
minimises water loss
from the leaf .

2. Sunken stomata 4 reduced number

of stomata in order to
✓
air movement
,
creating a layer of moisturethat ✓
transpiration .

Water
Reduced
3. number
of leafs : v5 A to Volume Ratio
.

v
loss

Harran Grass
4 .

Hairy leaves :
trichomes trap moist air
eg

5. Curled leaves 6 .
Succulent :
water stored in specialised
tissue
parenchyma .
Transport in Plants

Note small exist between xylem vessels known

:

"
passages
"

as
pits .

Allow air bubbles to

escape easily which
may
otherwise
>

prevent water
from flowing .

>

Regulate water 4 mineral ion contents between xylem

vessels .

> No
lignin exists in these Pits .

* Water on the
surroundings spongy mesophyll cells
is maintained Water Potential
via a
gradient .
Transport in Plants Casparian Strips

Casparian Strips:
Found in cells
Control
of Endo dermis .

water
transfer by :

1 .
Apo plastic Pathway
of adjacent cells via diffusion
as
I
•
>

Through cell walls .

8
A
8

É
of
2 .
Symplastic Pathway cells connected
a

ÉÉ
>

Through cytoplasm of adjacent

through the plasmodesma via osmosis
,
4
-

diffusion .

Made
from Sobering carbohydrate impermeable to water .

These
Casparian strips can block
symplastic apoplastic
,

or both
pathways depending
,
on how Soberin is
deposited .

Regulate movement
of water into the
xylem in the
foot .
Transport in Mammals
The
Heart

Heart:
An cardiac cells
organ comprising .

Myogenic involuntary contractions .

Semi lunar
-

Aorta
Yates
>
-

Pulmonary
Artery f.eptum
Pulmonary

.µ
•
Vein

Vena Cava
Right Atrium left Atrium
re muscular

eslj-i.H.iq?::::*
µ,µ,
"" Yates
or

- .
chordae
Tendineae > %Ñ" Y "

*
Coronary Arteries stem
from the Aorta .
Muscles
Transport in Mammals
Cardiac
Cycle

Cardiac Cycle:

i.
Deoxygenated blood
from the rest
of the body enters the

right atrium via the vena cava .

2 .
Once the threshold volume
of blood is achieved the muscles
,
of
walls
of the
right atrium contract .

The blood enters the ventricle

3 .

right .

4 .
The muscles
of tothe walls
of the right ventricle contract and
blood the the semi lunar
moves
pulmonary artery as -

valves open .

* Blood passes
from the Heart Twice

i. Heart >

Lungs
>
Heart
Pulmonary Circulation
2. Heart >
Body > Heart systemic Circulation
Transport in Mammals
Cardiac
Stages

i. Atrial systole :
Both atria contract .
Blood flows
from the atria

systole Contraction into the ventricles .

Backflow ofclosure
blood into
Diastole Relaxation the veins is prevented by the
of valves .

2. Ventricular systole : Both ventricles contract Blood .

flows from
the ventricles into the arteries .

Backflow
of blood is prevented by atrioventricular
Valles .

3. Ventricular Diastole :
Both ventricles relax .
Transport in Mammals Heart
Action

i. SAN sends out

excitation
waves
of
or
impulses .

2. Spread across both

Atria .

3 .
Both atria contract .

4. Non
bundle
conducting tissues
to
of His prevent
to ventricles
waves
go .

Time
5.
delay 0 I -0.2s
.

6 .
AVN sends out waves

of excitation which
pass
through Purkyne Fibres

reaching the Apex of

the Ventricles and then

spread upwards .
Transport in Mammals
Oxygen
Dissociation
Curve
I .

Haemoglobin Quaternary -

Hb + 40 ,
-
.

HB08

Looking 4 Unloading of 02
2 .
RBC

loading Unloading
@
Lungs @
Respiring cells
3. Concentration
=
of Oz
Partial Pressure
of 02

Curve rises steefly .

Cooperative Effect of O2
Small
change in 0, * 0 ,
+ Hb > Entire molecule
distorts This in turn
cone .
causes a
very slightly .

for
in saturation
large change .
makes it easier the 2nd
0, molecule to combine & so

on & so
forth .
Transport in Mammals
Forms of
Carbon
Dioxide
The Story of Carbon Dioxide:
Oxyhaemoglobin
Hb +0, Forms: I .

Simple solution
form dissolved in plasma .

Acid
Haemoglobonic 2 .
C0, + Hb Carb amino
haemoglobin
Hb + Ht
"
3 .

HC03 Hydrogen Carbonate Ions

carboxyhaemoglobin
Hb + CO s Within RBC >
Enzyme Carbonicanhydrase

£8
"
carbaminohaemoglobin t.CO, + 1-1,0 .
Haco, Carbonic Acid
Hb +
CO2 or

ÉÉ Ht
-

2 . Haco, -
-
+ HC0,
Hydrogen
ions carbonate
PROBLEMS :
"

i.
Decreasing pH of RBC since leaves RBC
HC0, leaves the cell and Ht
-

remains .

2.
Increasing
RBC
title
charge inside
.
Transport in Mammals Chloride
Shift

Chloride Shift:
Movement
of chloride ions into RBC
from blood plasma
,
to
balance the
of ions into the plasma from
-

movement HC03
RBC .

+
* Hb + H >
HHB Haemoglobonic Acid
0, and in
Helps in
Unloading of maintaining
>

RBC
the pH of .

Bohr’s Effect:
It is the decrease in
when C0, is
affinity of Hb
for 0 ,
that occurs

present .

> Graph : i. Moves to

right
@
lungs affinity of Hb with 0,
@ resp cells
O
ii. Moves downwards .

affinity of Hb with 0 , ✓

IE due to C02 cone .

ÉÉ
oÉ
É
Partial Pressure
of 0 ,
Transport in Mammals Capillaries

Transport of Materials between Capillaries:

> Fenestration
' '

Venite
' ' ' '

Arteriole
'

End . . . .
. . .
£
?d
>
Wall
of Capillary is one

cell thick .

00000
LIVER CELLS
'

i.
Hydrostatic Pressure at arteriole end .

2.
Only blood plasma passes
through the
fenestration to

form the tissue

fluid .

3. Glucose ,
amino acids and
oxygen diffuse down the
cone .

gradient into cells .

4.
Majority of H20 tissue fluid moves back into the

capillary down its water potential gradient by osmosis .

Transport in Mammals Arteries and
Veins

Artery
Tunica Media
i. Elastic Fibres
ii. Collagen
iii. Smooth Muscles

Tunica Externa
i.
Collagen Fibres
ii. Elastic Fibres

Vein
Tunica Media
i. Smooth Muscles
ii. Elastic Fibres

Tunica Externa
i. Collagen Fibres
Gas Exchange

Antagonistic Pair

oxygenated
blood
deoxygenated
blood

'

L
capillaries
Originate from Pulmonary Artery
Gas Exchange
Trachea:
Ciliated epithelium with Goblet cells .

Cilia beat back { forth to sweep

mucus & trapped particles up the throat .

Mucus traps dust particles .

Mucus cells .

Smooth Muscles
undergo rhythmic muscular contraction .

C- Shaped
cartilage in order to support the trachea walls
,

and prevent from collapsing .

Connective tissue .

Walls of Trachea
Gas Exchange
Gas Exchange in the Alveoli:

Alveoli coil & recoil due to elastic fibres .

Gas Exchange
smooth Ciliated Epithelial
Region of Airway Cartilage Goblet
Muscle cells Cells
Trachea - - - -

Bronchus - - - _

Terminal Bronchus ✗ - -
✗

Bronchioles ✗ ✓ -
✗

Alveolus Duct ✗ ✗ ✗ ✗

Alveoli ✗ ✗ ✗ ✗
Immunity
-
External
Defence a. HCl in stomach

b. Airway epithelium
Defence System c. Blood clotting

Internal Defense a. White Blood Cells

-

b. Antibodies
Identification:

* Cell
surface Antigens proteins on cell
surface membrane
are used for identification .
Cell to Cell
- -

Recognition
*
Antigens can be
self
-

antigens or non -

self antigens :

Antigens produced by the organism's own

body cells ,

are known as
self antigens .

Antigens not produced by the

organism's own
body
cells ,
are known as non -

self antigens .
Immunity
Vaccination:
Live attenuated pathogens dead .
> Non -

self Antigens
stimulates an immune
response .

Immune Response: Neutrophils

phagocytes
-

White Blood Cells

/
-

Lymphocytes
Macrophages
monocytes earlier primitive
-

macrophages

B- Lymphocytes T -

lymphocytes
B-Cells T -
Killer Cells

Phagocytosis:
i. Invaded cell produces help signal
Histamine , a .

2 .
This stimulates chemotaxis in a Neutrophil .

3. Bacterium attach directly to the Neutrophil Membrane ,

bacterium marked by antibody attach to receptor

for
antibody .

Endocytosis and bacteria surrounded

a. are
by phagocytic
Vacuole .

hydrolytic enzymes
s .
Fusion
of IY20mes la phagocytic Yacoole ,
DIGESTION .
Immunity
Lymphocytes:
Made : Bone Marrow
B- Cells Mature :
Bone Marrow

Made :
Bone Marrow
T Killer cells
Thymus Gland
-

Mature :

Origin and Maturation of B-Lymphocytes:

Immature B- Cells in bone marrow divide by mitosis .

Each B- Cell matures in bone marrow .

Production
of AntibodytheReceptors they & become

protein receptors in cell

surface membrane .

Mature B- Cells each with a

specific antibody receptor .
* The receptor is
specific to the
non -

self
it compliments the
Antigen & thus ,

shape .
Immunity

B-Cells Immune
Response
Immunity Immune Response

Helper Cells:
1st help secretes
cytokines
stimulate
2nd help phagocytosis
3rd help stimulate killer T-cells

ANTIGEN PRESENTATION display of antigens of pathogens on

the
surface of infected cell .

Immunity
Active Immunity Passive Immunity
short term
longterm Breastfeeding
colostrum
natural r

Natural Artificial antibody Natural

Artificial
Passive
Active
Immunity Immunity
Vaccination
Inject Antibodies {
Antitoxins
Immunity The Hybridoma Method

Plasma Cells cancer cells

+ ive production of antibodies five Rapid division
do not divide disease
-
iye
easily -
ive

Mixture
of Two Cells = HYBRIDONIA CELLS