Edexcel As Biology Revision Notes Unit 1
Edexcel As Biology Revision Notes Unit 1
Edexcel As Biology Revision Notes Unit 1
they are three main types of monosaccharides which you have to know in this leve
l which are
Pentoses - Such as ribose (with formula C5H10O5) and fructose Hexose - Such as a
lpha and beta glucoses
All members of monosaccharides are reducing since they have the aldehyde groups,
therefore they will cause a brick red persipitate to form when tested with bene
dict`s solution. 1 Designed & organized by: Mo Bahu Source: http://www.thestuden
troom.co.uk
Disaccharides
You would need to know 3 types of dissacharides in this level which is 1. Lactos
e - Formed between glucose and galactose and is bounded by 1,4 glycosidic bonds
(found in milk) 2. Maltose - Formed by 2 molecules of glucose and is bounded by
1,4 glycosidic bonds (found in starch after being hydrolysed) 3. Sucrose Formed
by a molecule of glucose and a molecule of fructose bounded by 1,2 glycosidic bo
nds (Found in most plant since it is used to transport sugary compounds) The for
mation of bonds between 2 monosaccharides is called condensation and the breakag
e of these bonds are called hydrolysis. Hydrolysis of these bonds can be brought
about by adding dilute HCl. Both lactose and maltose are reducing but sucrose i
s not a reducing sugar. Therefore disaccharides can or cannot be reducing. It is
not always a reducing agent.
Polyssacharides
There are three types of polyssacharides that we need to know at this level whic
h are
Starch
A polymer of alpha glucose and is bounded by 30% amylose (1,4 glycosidic bonds)
and 70% amylopectin (both 1,4 and 1,6 glycosidic bonds) It is used as a food sto
rage for plants and is built from the amyloplasts in the cytoplasm of plant cell
s. Starch is an important storage molecule since it is compact, insoluble in wat
er, inert to chemical reactions and is easily hydrolysed when required.
Glycogen
A polymer of alpha glucose with 1,4 glycosidic bonds but even more 1,6 glycosidi
c bonds compared to starch since it is even more branched.. It is used as an ene
rgy store in animals and is also found in bacterias Glycogen is an important sto
rage molecule since it is compact, insoluble in water, inert to chemical reactio
ns and is easily hydrolysed when required.
Cellulose
It is the constituent of cell walls and can be hydrolysed by ruminant animals by
the action of cellulase enzymes.. All polysaccharides are non reducing sugars.
Lipids
Lipids are basically fats and oild that contain elements of carbon, hydrogen and
oxygen An example of a lipid would be the triglyceride which is formed by glyce
rol and fatty acids .The bond formed is catalysed by the the process of condensa
tion between the OH groups of the glycerol and the fatty acids. The bonds formed
between them are the ester bonds. Since triglyceride itself is an ester. There a
re two types of fatty acids which are unsaturated and saturated fatty acids. An
example of a saturated fatty acid would be stearic acid and unsaturated would be
the oleic acid. The difference between saturated and unsaturated fatty acids ar
e the double bonds and the amount of hydrogen present at where saturated acids h
ave more hydrogen and no double bond present. The usages of triglycerides are im
portant energy stores, compact, insoluble in water, releases energy twice the am
ount of carbohydrates, and provides buoyancy for aquatic animals. The usages of
fatty acids include the formation of triglycerides and is also required for the
formation of phospholipids.
Phospholipids
Formed between fatty acids, glycerol and a phosphate group. The head is hydrophi
lic (soluble in water) but the tail is hydrophobic (insoluble in water). Therefo
re phospholipids are used as the main constituents of cell membranes
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Protein
Primary structure
It is the number , type and sequence of amino acids which makes up a polypeptide
chain
8Each amino acid is binded to another acid by peptide bonds by the process of co
ndensation. Amino acids are amphoteric since it has a zwitterion shapes.
Secondary structure
It is the shape of molecule formed when polypeptide chains are either coiled by
hydrogen bonds into a spiral springs ,the alpha helix or linked to form beta ple
ated sheets The alpha helix coils the polypeptide chains and are help in place b
y hydrogen bonds. An example of this would be keratin. The beta pleated sheets a
re formed by hydrogen bonds taking place between the CO and NH groups .It is ver
y strong but supple. An example would be collagen since it is fibrous. Insoluble
in water.
Tertiary structure
It is the folding of a polypeptide to form a globular shape. R groups of these p
roteins are bounded by ionic bonds, disulphide bridges and hydrogen bonds. An ex
ample would be enzymes.
Quaternary structure
A complex protein molecule which has more than one polypeptide chains bounded to
it. An example would be haemoglobin.
Experimental tests
Bear in mind that most of the unit 1 tests has at least 1 biological test questi
on which can yield up to 5 points and these tests should not be neglected.
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Benedict test
Test to confirm reducing properties of sugars. Add a few drops of benedict solut
ion into the sugar and boil. If it shows a brickred precipitate, a reducing suga
r is present. Since copper 2+ is reduced in copper +1 which shows are brick red
precipitate
Biuret test
Test to confirm the contents of protein or the presence of protein. Add an equal
amount of protein and biuret reagent. A purple-violet color would confirm the p
resence of proteins. This can be used as a qualitative test since the color is g
ets more intense as the protein content increases.
Sudan III test
To test the for the presence of fat Add equal amount of Sudan III and fat conten
ts together. A suspension of red liquid and white precipitate on the top would c
onfirm that there is fat present.
Nucleic acids
A nucleotide is made up of a pentose sugar ,and organic nitrogenous base and a p
hosphoric acid It is formed between the condensation of of a necleoside and a ph
osphate molecule Bonds which link a phosphate group to another phosphate group i
n a nucleotide is called the phosphodiester bond and the bond which links the ph
osphate and the nucleoside is the phosphoester bonds. There are 2 types of ribon
ucleotides which are RNA(the one containing ribonucleotides) and DNA(the one con
taining the deoxyribonucletides) There are two types of purines (Adenine, Guanin
e) and three types of pyrimidines (Uracil ,thymine and cystosine)
DNA replication
Replication of DNA is semi conservative, which means that the original DNA stran
d is reused to form new double stranded DNA. The process is as follows: 1. Helic
ase unwinds the double stranded DNA by breaking the hydrogen bonds.
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2. DNA attracts complementary bases onto the single stranded DNA which was used
as a template .(A is attracted to T) and (G is attracted to C) and vice versa in
the 5` direction to the 3` direction. The phophodiester linkages from other par
ts are joined by DNA Ligase from the 3` direction to the 5` direction In the end
, there will be two identical strains of DNA formed as a result. This is importa
nt in cell divisions of mitosis and meiosis
Protein synthesis
This process involves the synthesis of protein molecules by using genes found in
the DNA The process of transcription and translation is assisted by RNA(tRNA ,m
RNA and rRNA).They differ in three ways, which are 1. It is single stranded 2. I
t contains a pentose instead of a deoxyribose 3. The base thymine is replaced by
uracil The process starts off with transcription which involves the unwinding o
f the double stranded DNA molecule. This is then followed by the enzyme RNA poly
merase catalyzing the binding of mRNA bases to the DNA bases which are complemen
tary. After this is done, the mRNA is modified by adding a guanine cap at the 5`
end and a poly A being added to the 3` end of the mRNA. Thus it moves out of th
e nuclear envelope and into a ribosome in the cytoplasm or the rough endoplasmic
reticulum. After the mRNA reaches the ribosomes, a process known as translation
occus. mRNA then binds to a subunit of a ribosomes in such a way that the codon
s (3 units bases) are exposed. A unit of ribose consists of rRNA which has an en
tering point for 2 codons of mRNA whereelse a tRNA is a clover shaped molecules
which has 3 anticodons facing outwards. As the mRNA reaches the the ribosomes,2
tRNA molecules can be help at one time. The enzyme peptidyl transferase catalyse
s the formation of a peptide bond between 2 amino acids. After it is formed, tRN
A is moves out of the RNA and the product of the amino acids are moved into the
golgi apparatus with the help of a transport vesicle for further modification of
the amino acids.
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Enzymes
Enzymes are basically tertiary proteins which have an active sites which binds o
n to a substrate. The reaction causes bonds to be formed and broken much easier.
This is because enzymes act as organic catalysts which reduces the activation e
nergy needed for a reaction to go forward. The process is summarized as below :
Enzyme + Substrate ---enzyme-substrate complex---enzyme + products There are a few
factors which affect the rate at which the enzymes react, they are 1. Temperatu
re
The increase in temperature would increase the total kinetic energy of the su
bstrate and enzyme, thus the rate of collision increases and the rate of reactio
n increases. The opposite is shown if the temperature is reduced 2. pH
The decre
ase in pH would lead to excess H+ ions which will ionize the side groups in the
enzyme`s amino acids residue. This would lead to a change in its molecular struc
ture and cause the enzyme`s active site to be not complementary to the substrate
anymore. Thus the lower the pH, the more ionization and a less rate of reaction
. 3. Enzyme and Substrate concentration
The increase of any of the substate or c
oncentration would lead to a higher rate of collision and thus increases the rat
e or reaction 4. Inhibitors There are two types of inhibitors which are reversib
le inhibitors and non-reversible inhibitors
An irreversible inhibitor are inhibi
tors which has a shape which is complementary to the active site of an enzyme an
d therefore competes with the substrate for a reaction to proceed..this decrease
s the rate of reaction A non competitive inhibitors are inhibitors, this is usua
lly heavy metals which binds on to the enzyme and causes the enzyme to change it
s shape and loses its catalytic abilities. Therefore the rate of reaction is red
uced
Classification of enzymes
There are 5 types of enzymes which are 1. Oxidoreductase catalyses the process o
f oxidation and reduction 2. Transferase catalyses the transfer of one molecule
to another 3. Hydrolases catalyses the hydrolysis of a molecule 4. Lyase catalys
es the lysis (breakage) of a molecule 5. Ligase catalyses a formation of a bond
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ntroom.co.uk
Lipase
Catalyses the breakage of lipids into glycerol and fatty acids. Uses includes th
e enhancement of cheese ripening and biological detergents.
Practical : The production of immobilized enzymes
Mix sodium alginate solution with desired enzymes
a plastic syringe. Add this mixture dropwise into
r dehydration. Strain beads and rinse. Place into
he substrate. Collect the yield which is produced
A slower rate of reaction since the beads are now restraint of movement by the a
lginate solution
Aggregations of cells
An overview of a multicellular organism. Where cells make up the entire body. Th
is is as follows Cells-->Tissues->Organs-->individuals There are distinct differ
ences between an animal cell and a plant cell. Among the many, they are: 1. Vacu
oles which are found to be much larger in plant cells 2. Chloroplasts which are
found more abundantly in plant cells 3. Cell walls are usually present in plant
cells
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Cell membrane
The membrane functions as a passage of control for the substances into and out o
f the cells. The membrane is not only present on the surface of the membrane but
also at the membrane of organelles (mitochondrion, golgi apparatus, chloroplsts
etc.) It follows the fluid mosaic model at where fluid represents the phospholi
pid molecules having a fluid arrangement and mosaic represents the random arrang
ement of proteins, which moves above the phospholipid bilayer. The model shows p
hospholipids pointing head up. This is because the head section of the phospholi
pds is hydrophilic (soluble in water) where else the tail is hydrophobic (insolu
ble in water) Thus, having to know that, the bilayer only allows non-polar molec
ules to diffuse through a concentration gradient. Molecules which are sufficient
ly small (such as water, oxygen and carbon dioxide diffuses through the membrane
freely regardless of being polar or not. Polar molecules are only allowed to en
ter if they are incorporated into a carrier protein at where it is actively tran
sported into the cell or undergo facilitated diffusion (diffusion using a protei
n molecule). Glycolipids are also present on the cell surface membrane since it
allows cell recognition and also to promote an immune response Carbohydrates and
cholesterol functions to reduce the fluidity of the membrane and maintain its s
tability to ensure that no leaking occurs. Proteins which are present can ether
be intrinsic or extrinsic and is important in maintaining the stability of the m
embrane.
Endoplasmic Reticulum (ER)
Smooth ER
Important at protein synthesis since it has ribosomes at the top of its surface.
Golgi apparatus
It functions to modify proteins which are produced from the process of protein s
ynthesis After the synthesis of the proteins, the product is brought out of the
cells with the cell through a secretary vesicle. As the secretory vesicles fuses
with the membrane, it releases its contents into the surroundings through the p
rocess of exocytosis. The Golgi apparatus is also important in the process produ
cing lysosomes, which contains hydrolytic enzymes. These hydrolytic enzymes caus
e the breakdown of unwanted organelles. It is also important to digest phagocyti
c vesicles.
Nucleus
Contains a double layers membrane which separates the genetic material from the
cytoplasm.The nuclear membrane sometimes contains ribosomes for protein synthesi
s. Among the contents of the Nucleus are chromosomes, chromatin, histones, rRNA.
Mitochondrion
It is rod shaped with a double layered membrane consisting of cristae for increa
sing the surface area.The membrane of the mitochondria is called the matrix. It
is involved in the production of ATP from cellular respiration.
Chloroplasts
Contains a double layered membrane with molecules of chlorophyll anchored on it.
It also has stacks of granum (formed by stacks of thylakoids) and its cytoplasm
Is called the stroma. It also contains starch, lipid droplets and circular DNA.
Involved in the process of photosynthesis.
Microtubules
Fine tubular organelles which contribute to the network of fibrous protein. It i
s necessary for microtubules to be present since it provides the maintenance and
shape of certain organelles such as centrioles and is also present in the flage
llum of some bacterias.
Cell walls
In fungi, its cell wall composition is made out of chitin. In bacteria, its cell
wall composition is made out of murein In plant cell walls, its composition is
made out of cellulose. The main function of plant cell walls are to provide mech
anical strength and the resist expansion of plant cells when subjected to high h
ydrostatic pressure.
The difference between prokaryotic cells and eukaryotic cells
Prokaryotes are basically cells with a smaller size wherelse eukaryotic are larg
er Prokaryotes have smaller (70s) ribosomes whereas eukaryotes have larger (80s)
ribosomes Prokaryotes lack a true nucleus whereelse a eukaryotes has a real nuc
leus present Prokaryotes have no membrane bounded organelles whereas eukaryotes
do. Flagellum present in prokaryotes lacks a 9+2 arrangement of microtubules whe
reelse eukaryotes does not.
Transfer across cell membranes
Diffusion
There are 2 types of diffusion which are facilitated diffusion and simple diffus
ion. Simple diffusion involves the transfer of molecules across a membrane or ba
rrier following a concentration gradient. Facilitated diffusion involves the tra
nsfer of molecules across a barrier or membrane following a concentration gradie
nt with the help of a protein carrier. This is because as the molecules bind on
the the protein, it changes its shape in a way that it allows the molecule to be
detached form the protein and get released into the cytoplasm of the cell or vi
ce versa.
Osmosis
Separated into 3 phases which are the G1,S and G2 phase. In the G1 stage, the ce
ll is undergoing a period of rapid growth. In the S stage, DNA molecules are rep
licating and therefore the number of chromosomes are now doubled here. Histones
are built up and the chromosomes are divided into two chromatids. In the G2 stag
e, more cell growth is taking place at where some organelles divide and there is
an accumulation of energy stores
Prophase
This phase can be seen clearly through a light microscope since it is positively
charged and it takes up the orcein staind much easier. Chromosomes become short
er and thicker on this stage, nucleoli starts to disappear.
Metaphase
Chromosomes get attached to the spindle fibres and the chromosomes align at the
equator of the cell
Anaphase
Centromers divide and the spindle fibres shorten and pulls the centromers to opp
osite poles. (attracted by centrioles)
Telophase
Chromosomes begin to uncoil from histones and the nuclear envelopes begins to fo
rm.
Cytokinesis
A process whereby furrows are formed after the process of anaphase .It only occu
rs in animal cells .A plant cell forms cell walls between the two nucleus formed
to separate the cells.
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