The complex formed when two or
more atoms bond together
What is a molecule?
What are covalent bonds?
What are the bonding rules for
carbon, nitrogen, oxygen and
hydrogen atoms?
What is an ion?
What is an ionic bond?
Bond that occur when two atoms
share a pair of electrons. The
electrons used to form bonds are
unpaired and present in the outer
orbitals of the atoms.
• Carbon atoms form 4 bonds
Electrolytes
• Nitrogen atoms form 3 bonds
• Oxygen atoms form 2 bonds
• Hydrogen atoms form 1 bonds
An atom or molecule with an overall
electric charge because the total
number of electrons is not equal to
the total number of protons
A chemical bond that involves the
donating of an electron from one
atom to another, forming positive
and negative ions held together by
the attraction of the opposite
charges
An atom or molecule that loses one
or more electrons giving it a net
positive charge.
What is a cation?
An atom or molecule that gains one
or more electrons giving it a net
negative charge.
What is an anion?
What are ions in solution
called?
• Calcium ions (Ca2+)
• Sodium ions (Na+)
• Potassium ions (K+)
List all of the important cations • Hydrogen ions (H+)
in living organisms • Ammonium ions (NH4+)
• Nitrate ions (NO3-)
• Hydrogen carbonate ions (HCO3-)
• Chloride ions (Cl-)
List all of the important anions • Phosphate ions (PO43-)
in living organisms • Hydroxide ions (OH-)
 1. Nerve impulse transmission and • In covalent bonds the atoms are
What are the following cations muscle contractions
not always shared equally by the
necessary for? 2. Nerve impulse transmission and atoms of different elements

kidney function
• The atoms with the greater share
1. Calcium ions 3. Nerve implies transmission and Why are some molecules of negative electrons will be
2. Sodium ions stomatal opening
polar? slightly negative compared with
3. Potassium ions 4. Catalysis of reactions and pH the other atom in the bond, which
4. Hydrogen ions determination
will be slightly positive

5. Ammonium ions 5. Production of nitrate ions by • Polar molecules have regions of

What are the following anions
necessary for?
bacteria negativity and regions of positivity
1. Nitrogen supply to plants for • Oxygen always has a much
amino acid and protein formation
greater share of electrons in an O-
2. Maintenance of blood pH
H bond

3. Balance positive charge of Why is water is polar • Many organic molecules contain
sodium and potassium ions in molecule? hydroxyl (OH) groups, and so are
1. Nitrate ions
cells
slightly polar; water is an example
2. Hydrogen carbonate ions 4. Cell membrane formation,
3. Chloride ions nucleic acid and ATP formation,
4. Phosphate ions bone formation
• Hydrogen bonds are relatively
5. Hydroxide ions 5. Catalysis of reactions and pH weak interactions

determination • They are caused by polar

What are hydrogen bonds, and molecules interacting with each
• Carbohydrates - carbon, what causes them? other and forming bonds -
hydrogen, and oxygen usually in hydrogen bonds
the ration Cx(H2O)x

List the 4 biological molecules • Lipids - carbon, hydrogen, and

and the element present in oxygen

• Liquid

each of them • Proteins - carbon, hydrogen, • Density

oxygen, nitrogen, and sulphur

Solvent

•
• Nucleic acids - carbon, hydrogen, • Cohesion and surface tension

oxygen, nitrogen, and phosphorus List the properties of water

• High specific heat capacity

• In carbohydrates the monomers • High latent heat of vaporization

are sugars (saccharides)

What are the monomers in • In proteins the monomers are

carbohydrates and proteins amino acids
called?
 • The hydrogen bonds between • As it is polar, the positive and
water molecules make it more negative parts of the water
difficult for them to escape to molecules are attracted to the
Why is water a liquid at room become a gas
oppositely charged parts of the
temperature? solute

Why is water a good solvent?

What is the importance of
water being a liquid at room
temperature, to living
What is the importance of
organisms?
• Water molecules cluster around
the charged parts of the solute
molecules or ions, which helps to
• Provides habitats for living things separate them and keep them
in rivers, lakes and seas
apart
• Forms a major component of the
tissues in living organisms
• Molecules andirons can move
around and react together in water
• Provides a reaction medium for
chemical reactions
e.g. as in the cytoplasm of cells,
• Provides an effective transport water being a good solvent to which is >70% water

Describe how the density of
water changes, as H2O
medium e.g. in blood and vascular
tissue
Usually the solid is more dense than
the liquid form of a substance.
• Water molecules demonstrate
However ice is less dense than
water because as water goes from
living organisms? • molecules and ions can be
transported around living things
whilst dissolved in water
cohesion because hydrogen
bonding between the molecules
pulls them together

changes state 4C to freezing point, the water • Water molecules demonstrate

What is the importance of
molecules form a structure that is Describe cohesion and surface surface tension because they are
less dense than liquid water tension of water more attracted to the water
molecules beneath them than air
• If water was less dense, aquatic molecules above, so the water
organisms would find it very contacts, giving the surface of the
difficult to float
water the ability to resist a force
applied to it
Ice floats on water so:

water’s density to living
organisms?
• Aquatic organisms have a stable
environment to live through in
winter
What is the importance of
• Ponds are insulated against
• Columns of water in plant vascular
tissue are pulled up the xylem
tissue together from the roots due
cohesion and surface tension to cohesion

extreme cold because the ice layer of water to living organisms? • Insects like pond-skaters can walk
reduces heat loss from the pond on water due to surface tension

Why does water have a high
specific heat capacity?
What is the importance of the
Define the following:
high specific heat capacity of
water to living organisms?
Why does water have a high
latent heat of vaporisation?
What is the importance of the
high latent head of
vaporisation of water to living
organisms?
What is the importance of
water’s role as a reactant to
living organisms
• Water molecules are held together
quite tightly by hydrogen bonds
elements carbon, hydrogen and
• Therefore you need to put in a lot
of heat energy to increase their
kinetic energy and temperature
saccharides or sugars
• This means that water doesn’t
heat up or cool down easily
• Living things need a stable
temperature for enzyme-controlled
reactions to happen properly
2. A molecule comprising two
• Aquatic organisms need a stable
environment in which to live
Because the water molecules are
held together by hydrogen bonds, a
relatively large amount of energy is
needed for water molecules to
evaporate
Water can help to cool living things
and keep their temperature stable
e.g.
2 variations
• Mammals are cooled when sweat
evaporates
below carbon 1
• Plants are cooled when water
evaporates from mesophyll cells
It is a reactant in reactions such as
photosynthesis, and in hydrolysis
reactions such as digestion of
starch, proteins and lipids
water molecule is formed (lost)
• Plays a very important role in the
digestion and synthesis of large
biological molecules
Organic polymers composed of the
oxygen, usually in the ration
Cx(H2O)y. Also known as
What are carbohydrates?
1. A single sugar molecule e.g.
glucose, fructose and ribose
1. Monosaccharide monosaccharides joined
2. Disaccharide together by a glycosidic bond
3. Polysaccharide 3. A polymer made up of many
monosaccharides e.g. glycogen,
cellulose and starch
• C6H12O6
• Hexose monosaccharide (because
it has 6 carbons)
• Polar and soluble in water due to
the hydrogen bonds that form
between the OH group and water
molecules
Describe glucose
• Means glucose is dissolved in the
cytosol of the cell
• Alpha glucose - OH group is
• Beta glucose - OH group is above
carbon 1
• The OH groups on C1 and C4
reacted forming a 1,4 glycosidic
How do alpha glucose bond (covalent)
• Condensation reaction because a
molecules react with each
other?
 1. Maltose
• Found in plants

What do the following

2. Sucrose
• Alpha glucose

combinations form? 3. Lactose

• Has glycosidic bonds between C1
1. a-glucose + a-glucose 4. Cellobiose and C4, and also has branches
2. a-glucose + fructose formed by glycosidic bonds
3. B-galactose + a-glucose Describe amylopectin between C1 and C6

4. B-glucose+ B-glucose • Coils into a spiral shape held

together by hydrogen bonds, but
• Sugars that contain 5 carbon with branches coming out of the
atoms
spiral
What are pentose • e.g. ribose which is the sugar
present in RNA nucleotides
A branched polysaccharide formed
monosaccharides? Give from alpha glucose. A chemical
examples • e.g. deoxyribose which is the
sugar present in DNA nucleotides energy store in animal cells
What is glycogen?

A polysaccharide formed from alpha

glucose molecules either joined to
form amylose or amylopectin. Found
in plants • Found in animals

What is starch?
• Like amylopectin with glycosidic
bonds between C1 and C4, and
branches formed by glycosidic
bonds between C1 and C6

• Found in plants
• The C1 C4 bonded chains are
• Alpha glucose
Describe glycogen smaller than in amylopectin so
glycogen has less tendency to coil

• Glycosidic bonds between C1

andC4
• Has more branches than
amylopectin making it more
• Coils into a spiral shape held
compact

Describe amylose together by hydrogen bonds

• OH groups on C2 inside of the • Easier to remove monomer units

coil, making the molecule less as there are more ends
soluble and allowing hydrogen
bonds to form to maintain the
coil’s structure
 • The OH groups on C1 and C4 are Lipids composed of one glycerol
to far away to react, so each (C3H8O3) molecule and three fatty
alternate beta glucose molecule acids. Fatty acids are carboxylic
How do beta-glucose must be turned upside down to What are triglycerides? acids that consist of a carboxyl
molecules react with each reach
group (-COOH) which a hydrocarbon
other? • It is unable to could or form chain attached.
branches

• A straight chain molecule called

cellulose is formed

• Cellulose molecules make

hydrogen bonds with each other
forming microfibrils
Formation of a triglyceride
• Microfibrils join together to form
Describe cellulose macrofibrils that combine to
produce fibres

• The fibres are strong and insoluble • The hydroxyl groups in the fatty
and are used to make cell walls acid molecule and glycerol
• Microfibrils and macrofibrils have molecule react

very high tensile strength because • This leads to the formation of 3

of the glycosidic bonds and water molecules and bonds
hydrogen bonds
between the fatty acid and
How are triglycerides formed? glycerol molecule

Why is cellulose a good • macrofibrils run in all directions,

criss-crossing the wall for extra • The bonds are called ester bonds,
material for cell walls? strength
and the reaction is called
• Space between macrofibrils for esterification

water and mineral ions to pass in • Esterification is an example of a

and out of the cell, making the cell condensation reaction
wall full permeable
• Fatty acid chains that have no
Non-polar macromolecules contains double bonds between the carbon
the elements carbon, hydrogen and atoms are saturated, and vice
What is the difference between
oxygen. Soluble in alcohol rather versa

saturated and unsaturated

than water. Include triglycerides, • If there’s 1 double bond =
What are lipids? triglycerides?
phospholipids and sterols. monounsaturated

• If there’s 2 or more double bonds

= polyunsaturated

How does the presence of
double bonds in unsaturated
triglycerides cause?
What type of triglycerides do
plants contain?
Which type of triglycerides are
healthier?
What are phospholipids?
• Changes the bond angle and
causes the molecule to kink or
bend
• Therefore the molecules cannot
pack so closely together
• Makes them liquid at rtp rather
than solid, so they are oils rather
than fats
Unsaturated triglycerides, which
normally occur as oils
hydrophobic and repelled by water
Unsaturated triglycerides are
healthier for human than
triglycerides or (solid) fats.
Modified triglycerides, where one
fatty acid has been replaced with a
phosphate group. They are found in
the cytoplasm of very cell.
Phospholipid
• Have a non-polar end (the fatty
What are the characteristics of • Have a charged head (the
phospholipids?
How do phospholipids interact
with water?
How do the characteristics of
phospholipids help in the
formation of cell membranes?
acid chains) which are
phosphate PO43-) which are
hydrophilic and attracted to water
• Form a layer on surface of water
with phosphate heads (hydrophilic)
in the water and fatty acid tails
(hydrophobic) sticking out
• Can form structures based n a
bilayer with all the hydrophobic
tails pointing towards the centre of
the sheet, protected by from the
water by hydrophilic heads
• The bilayer arrangement means
that they can separate the aqueous
environment in which cells usually
exist, from the aqueous cytosol
within the cells

What are sterols?
Describe the characteristics of and the rest of the molecule is
sterols
What is cholesterol?
What is the importance of
cholesterol in the formation of
cell membranes?
What is the importance of
cholesterol in regulating the
fluidity of cell membranes?
Steroid alcohols. Complex alcohol
molecules based on a 4 carbon ring
structure with a hydroxyl (OH) group
at one end.
Have a dual hydrophilic/hydrophobic
characteristics. The hydroxyl group
is polar and therefore hydrophilic,
hydrophobic.
• A type of sterol
• Buoyancy for aquatic animals like
• The body primarily manufactures it
in the liver and intestines
• Vitamin D, steroid hormones and
bile are all manufactured using
cholesterol
• Positioned between the
phospholipids with the hydroxyl
group at the periphery of the
membrane
polypeptides and thus proteins
• Adds to the stability of cell
membranes
Keeps membranes fluid at low
temperatures and stops them
becoming too fluid at high
temperatures
• Membrane formation and the
creation of hydrophobic barriers
• Hormone production
What are the roles of lipids? • Electrical insulation necessary for
(Due to their non-polar nature) impulse transmission
• Waterproofing, e.g. in birds’
feathers and on plant leaves
• Long-term energy storage
Stored under the skin and around
vital organs where they provide:
What are the roles of • Thermal insulation to reduce heat
triglycerides in particular? loss, e.g. in penguins
• Cushioning to protect vital organs
e.g. heart and kidneys
whales
1. One or more polypeptides
arranged as a complex
Define the following: macromolecule
1. Proteins 2. Chains of two or more amino
2. Peptides acid molecules
3. Peptide bond 3. Bond formed between two
4. Amino acid amino acids
4. Monomer used to build

Amino acid
• The hydroxyl in the carboxylic acid
group of one amino acid reacts
with a hydrogen in the amine
group of another amino acid
of proteins?
Describe what happens when
• A peptide bond is formed between
two amino acids react together the amino acids and water is
produced (condensation reaction)
• The resulting compound is a
dipeptide
• When many amino acids are joined
together by peptide bonds
• This reaction sis catalysed by the
enzyme peptide transferase
When is a polypeptide formed?
present in ribosomes, the sites of
protein synthesis
What happens to the R-groups
of the amino acids when the
amino acids react?
What does the presence of
different sequences of amino
acids lead to?
What is the primary structure
What is the secondary
structure of proteins?
• Different R-groups interact with
each other (R-group interactions)
forming different types of bond
• These bonds lead to polypeptides
folding into complex structures
(proteins)
Different structures with different
shapes being produced
The very specific shapes of proteins
are vital for the many functions
proteins have within living organisms
• The sequence in which the amino
acids are joined
• Directed by information carried
within DNA
• The amino acids in the sequence
will influence how the
polypeptide’s fold to give the
proteins final shape, and
determine its function
• The only bonds here are peptide
bonds
• The oxygen, hydrogen, and
nitrogen atoms of the amino acids
(excluding R groups) interact
• A result of hydrogen bonds and
forms at regions along long protein
molecules depending on the
amino sequences

What are the two types of
secondary structure?
What is tertiary structure?
List the interactions that occur
between R-groups
• Alpha Helix - Hydrogen bonds • Protein structure where a protein
form within the amino acid chain, consists of more than 1
pulling it into a coil shape called polypeptide chain, e.g insulin has
an alpha-helix
a quaternary structure
• Results from the association of 2
• Beta Pleated Sheet - Polypeptide or more individual proteins called
bonds lie parallel to each other subunits
joined by hydrogen bonds, forming
What is quaternary structure?
• The interaction between subunits
sheet-like structures.The pattern are the same as in tertiary
formed by individual amino acids structure except between different
makes the structure appear protein molecules rather than
pleated within one molecule
• The protein subunits can be
• The folding of a protein into its identical or different
final shape
• Often includes sections of • Proteins are assembled in the
secondary structure
aqueous environment of the
• The coiling or folding of sections cytoplasm
of proteins into their secondary • The way a protein will fold also
Describe hydrophilic and
structures brings R-groups of depends on whether the R-groups
different amino acids closer
hydrophobic interactions in are hydrophilic or hydrophobic
together so they can interact proteins • Hydrophilic groups arena the
outside, whilst hydrophobic are on
• Hydrophobic and the inside of the molecule (away
hydrophilicinteractioncs - weak from the cytoplasm)
interactions between polar and
non-polar R-groups
• Globular proteins
• Hydrogen bonds - these are the • Conjugated proteins
weakest of bonds formed
• Fibrous proteins
• Ionic bonds - stronger than List the types of proteins
hydrogen bonds and form
between oppositely charged R-
groups
• Disulfide bonds/bridges - covalent
and the strongest of the bonds but
only form between R-groups that
contain sulphur atoms

What are globular proteins?
Describe how the structure of
Insulin is suited to its function
What are conjugated proteins?
Compact, spherical, water-soluble
proteins
red blood cells
• Form when proteins fold into their
tertiary structures so that the
hydrophobic R-groups on the
amino acid are kept away from the
aqueous environment
• Hydrophilic R-groups on the
outside of the protein meaning the
proteins are soluble in water
reversibly with an oxygen molecule
• e.g. Insulin
• Globular protein
• Hormone involved in regulation of
blood glucose concentration
• A quaternary protein containing 4
• Hormones are transported in the
bloodstream so need to soluble
• The presence of Fe2+ ions in the
• Hormones have to fit into specific
receptor on cell-surface
membranes to work, therefore
need to have precise shapes
Globular proteins that contain a
prosthetic group.
components, so catalase makes
Lipids or carbohydrates can
combine with proteins forming
lipoproteins or glycoproteins. Metal
ions and molecules derived from
vitamins also form prosthetic groups
proportion of amino acids with
• e.g. Haemoglobin and Catalase
both contain prosthetic harm groups
(Fe2+)
Describe how the structure of
haemoglobin makes it suited
to its function
Describe how the structure of
catalase makes it suited to its
function
What are fibrous proteins?
• Red, oxygen-carrying pigment in
• Quaternary protein made from 4
polypeptides (2 alpha and 2 beta
subunits)
• Each subunit contains a prosthetic
hem group
• The Fe2+ ions in the haem groups
are each able to combine
which enables haemoglobin to
transport oxygen around the body
• An enzyme
prosthetic harm groups
haem groups allow catalase to
interact with hydrogen peroxide
and speed up its breakdown
• Hydrogen peroxide is a common
byproduct of metabolism but
damaging to cells and cell
sure it doesn’t accumulate
Long insoluble, structural proteins
• Due to the presence of a high
hydrophobic R-groups in their
primary structures
• Amino acid sequence in primary
structure is usually very repetitive
leading to very organised
structures
• Are NOT folded into complex 3D
shapes like globular proteins
• E.g. Keratin, Elastin and Collagen

Describe how the structure of
keratin is suited to its function
Describe how the structure of
elastin is suited to its function
Describe how the structure of
collagen makes it suited to its
function
• Group of fibrous proteins 1. Add iodine solution (in
presenting hair, skin and nails
potassium iodide) to a sample
• Large proportion of the sulfur- 2. If starch is present, you will see a
containing amino acid cysteine colour change from yellow-
leading to many strong disulphide brown to blueback
bonds forming strong, inflexible, Describe the test for starch
insoluble materials
• When dissolved in potassium
• Hair contains fewer disulphide iodide, the iodine (I2) forms a
bonds than nails, so is more triiodide I3-, which slips into the
flexible middle of the amylose helix,
causing a colour change
• Fibrous protein found in elastic
fibres
1. Place the sample in a boiling
• Elastic fibres are present in the tube. If its not liquid, grind it up
walls of blood vessels and in the or lend it in water
alveoli of the lungs
2. Add an equal volume fo
• Give these structures flexibility to Benedict’s solution
expand when needed but also to 3. Heat the mixture gently in a
return to their normal size
boiling water bath for 5 minutes
• Quaternary protein made from Describe the test for reducing
many stretch molecules called sugars (all monosaccharides Blue > Green > Yellow > Orange >
tropoelastin and some disaccharides) Red
• Fibrous protein
• Benedict’s reagent is an alkaline
• Connective tissue found in skin, solution of copper (II) sulphate
tendons, ligaments and the
• The more reducing sugar present,
nervous systems
the more brick-red precipitate
• Many different forms but all are formed and the less blue Cu2+
made up of 3 polypeptides wound ions left in solution
together in a long and strong rope-
like structure
• Like rope, collagen has flexibility

Describe the test for non-
reducing sugars
Describe the test for lipids
Describe the test for proteins
1. Do Benedict’s test for reducing Large polymers formed from
sugars, the result will be nucleotides. Contain the elements
negative
carbon, nitrogen, hydrogen,
2. Sucrose is the most common What are nucleic acids? phosphorus, and oxygen.
non-reducing sugar
3. If sucrose is first boiled with
dilute hydrochloric acid then it’ll
give a positive result when
warmed with Benedict’s solution
• A pentose monosaccharide
containing 5 carbon atoms
• This is because the sucrose has • A phosphate group, (PO42-) and
been hydrolysed by the acid to inorganic molecule that is acidic
Describe the composition of
glucose and fructose, both and negatively charged
reducing sugars
nucleotides
• A nitrogenous base - a complex
organic molecule containing 1 or 2
1. Mix the sample with ethanol
carbon rings in its structure, as
2. The resulting solution is mixed well as nitrogen
with water and shaken
3. If a white emulsion forms as a • By condensation reactions
layer on top the solution, this • Phosphate group at the 5th carbon
indicated the presence of a lipid
of the pentose sugar (5’) of one
4. If the solution remains clear, the nucleotide forms a covalent bond
test is negative with the hydroxyl (OH) group at the
How do nucleotides link 3rd carbon (3’) of the pentose
1. Add Biuret A (sodium hydroxide)
together to form a sugar of another nucleotide
and then Biuret B (copper
polynucleotide? • These bonds are called
sulphate) to the sample
phosphodiester bonds
2. If a protein is present, the colour
• Forms a long, strong sugar-
changes from light blue to lilac/ phosphate ‘backbone’
mauve
• Phosphodiester bonds are broken
by hydrolysis
The molecule responsible for the
storage of genetic information
• The sugar is deoxyribose, which
What is Deoxyribonucleic acid has 1 less oxygen atoms than a
(DNA) ? ribose sugar
• The nucleotides each have 1 of 4
different bases: Adenide, Thymine,
Guanine, or Cytosine
 • Single-ringed, nitrogenous bases • A small pyrimidine base always
that form part of a nucleotide
binds to a larger purine base; this
• Smaller bases
arrangement keeps a constant
What are pyrimidines? • Thymine (T) and Cytosine (C) What are the consequences of
distance between the DNA
backbones, resulting in parallel
complimentary base pairing? polynucleotide chains

• DNA always has equal amounts of

adenine and thymine, and cytosine
• Double-ringed, nitrogenous bases and guanine
that form part of a nucleotide

Polynucleotide molecules involved in

• Larger bases

the copying and transfer of genetic

What are purines? • Adenine (A) and Guanine (G)
information from DNA.

What is Ribonucleic acid?

(RNA) The monomers are nucleotides
consisting of a ribose sugar and 1 of
four bases: Adenine, Uracil,
• Made up of 2 strands of
polynucleotides coiled into a helix
Cytosine, or Guanine
• The 2 strands are held together by Similarities:

hydrogen bonds between the • RNA nucleotides form polymers in

Describe the double helix bases
the same way as DNA nucleotides
structure of DNA • Each strand has a phosphate - by the formation of
group (5’) at one end, and a phosphodiester bonds

hydroxyl group (3’)at the other end

What are the similarities and
• The 2 parallel strands run in differences between DNA and Differences:

opposite directions - antiparallel RNA? • In RNA the pentose sugar is

Specific hydrogen bonding between ribose, meanwhile in DNA it’s
nucleic acid bases. A binds to T or deoxyribose

U, C binds to G
• In RNA, the thymine base is
What is complementary base replaced with Uracil
pairing? • A and T form 2 hydrogen bonds so The semi-conservative process of
always join with each other
the production of identical copies of
• C and G form 3 hydrogen bonds DNA molecules
so always join with each other
What is DNA replication?
 DNA replication results in one old The sequences of baes in DNA are
strand and one new strand present the ‘instructions’ for the sequences
in each daughter DNA molecules of amino acids in the production of
What is semi-conservative proteins
What is the genetic code?
replication?

1. The enzyme DNA helicase The genetic code is a sequence of

travels along the DNA backbone, three nucleic acids bases, called a
catalysing reactions that breaks codon. Each codon codes for one
the hydrogen bonds between amino acids.

complimentary base pairs

What is a triplet code?
2. After the ‘unzipping’, free DNA A section of DNA that contains the
nucleotides will then pair with complete sequence of baes
their complimentary bases, (codons) to ode for an entire protein
Describe the process of semi-
which have been exposed as the is called a gene.
conservative replication strands separate

3. Hydrogen bonds are formed • There are 64 different base triplets

between the new complimentary or codons possible, but there are
bases
only 20 amino acids

Why is the genetic code a • Therefore, many amino acids can

4. The enzyme DNA polymerase
catalyses the formation of
phosphodiester bonds between
adjacent new nucleotides
A change in the genetic material
which may affect the phenotype of
the organism.
that codes for a protein (if it’s in
What is a mutation?
Happen due to random error in the
degenerate code?
be coded for by more than one
codon
• There’s a start codon (ATG) that
signals the start of a sequence
the middle of a gene it codes for
methionine)

replication of DNA that lead to a How are genes read? • Having a start codon means that
change in the sequence of bases codons are read ‘in frame’, so the
genetic code is non-overlapping

• There are 3 stop codons that don’t

code for any amino acids, and
signal the end of the sequence
 The process of copying smaller • Maintaining the structural stability
sections of DNA base sequence to of the protein synthesis sequence

produce smaller molecules of • Biochemical role in catalysing the

What is transcription? mRNA, which can be transported What is the role of rRNA? reaction
out of the nucleus via the nuclear
pores, to the site of protein
synthesis

1. A gene unwinds and unzips, • Binds to a specific site on the

aided by DNA helicase, and the small subunit of a ribosome

hydrogen bonds between • The ribosome holds mRNA in

complimentary nucleotide bases What happens to mRNA after it position while it is translated into a
break
has left the nucleus? sequence of amino acids

2. The sense strand (5’ to 3’) codes • This process is called translation
for the protein, whilst the
antisense strand (3’ to 5’)acts as
the template strand during The process by which the
transcription
complementary code carried by
3. RNA polymerase catalyses the mRNA is decoded by tRNA into
Describe the process of
formation of temporary hydrogen What is translation? sequence of amino acids. This
transcription bonds between RNA nucleotides occurs at a ribosome
and their complimentary DNA
bases on the template strand

4. The strand of RNA produced is

complimentary to the template Form of RNA that carries an amino
strand, so is a copy of the acid specific to its anticodon to the
sense/ coding strand
correct position along mRNA during
5. Messenger RNA (mRNA) passes translation

out of the nucleus, through the

nuclear envelope, whilst the DNA • Single stranded polynucleotides,
double helix reforms but can twist into a hairpin shape

What is transfer RNA (tRNA)?

• At one end is a trio of nucleotide
• 2 subunits, one large and one bases that recognises and
small
attaches to a specific amino acid

• Almost equal amounts of protein • At the loop is another triplet of

What are ribosomes made up and ribosomal RNA (rRNA)
of? (eukaryotic cells) bases called an anticodon that is
complementary to a specific
codon of bases on the mRNA
 1. mRNA binds to the small subunit • Synthesis - e.g. of large molecules
of the ribosome at its start such as proteins

codon (AUG)
• Transport - e.g. pumping
What are the 3 main types of
2. A tRNA with the complementary molecules or ions across cell
anticodon (UAC) binds to the
activity cells require energy membranes by active transport

mRNA start codon. This tRNA for? • Movement - e.g. protein fibres in
carries the amino acid muscle cells that cause muscle
methionine
contraction
3. Another tRNA with the
complementary anticodon, and Adenosine diphosphate

carrying an amino acid, binds to

the next codon on the mRNA. A A nucleotide composed of a
maximum of 2 tRNAs can be nitrogenous adenine base, a
bound at the same time
pentose sugar and 2 phosphate
What is ADP? groups

Describe how translation 4. The 1st amino acid (methionine)

happens at a ribosome is transferred to the amino acid
on the 2nd tRNA by the Formed by the hydrolysis of ATP,
formation of a peptide bond. releasing a phosphate ion and
This is catalysed by the enzyme energy
peptidyl transferase, which is an • The instability of the phosphate
rRNA component of the bonds

ribosome
• Fats and carbohydrates are better
5. The ribosome then moves along long-term energy stores

the mRNA, releasing the 1st • Energy released in the breakdown

tRNA. The 2nd tRNA becomes
the 1st
Why is ATP not a good long-
6. Stages 3-5 are repeated until the
of these molecules (a process
called cellular respiration) is used
term energy store? to create ATP

ribosome reaches the end of the • A phosphate group is reattached

mRNA at a stop codon, and the to an ADP molecule
polypeptide is released (phosphorylation which is an
Adenosine triphosphate
example of a condensation
reaction)
A nucleotide composed of a
nitrogenous adenine base, a
What is ATP? pentose sugar, and 3 phosphate
groups. The ‘universal energy
currency’ for cells, because it is
used for energy transfer in all cells.
 • Due to the instability of ATP
• Small - moves easily into, out of,
• Instead ATP is rapidly reformed by and within cells

the phosphorylation of ADP

• Water soluble - energy requiring
Why do cells not store large • Interconversion of ATP and ADP is processes happen in aqueous
happening constantly in all living environments

amounts of ATP? cells, so cells don’t need a large • Contains bonds between
store of ATP
phosphates with immediate
What are the properties of ATP
• ATPis a good immediate energy energy: large enough to be useful
store
that make it suited to carry out for cellular reactions, but not so
its function in energy transfer? large that energy is wasted as heat

1. When a cell needs energy, ATP is

• Releases energy in small quantities
broken down to ADP and Pi
- quantities are suitable to most
2. In the hydrolysis reaction, a cellular needs, so that energy is
phosphate bond is broken and not wasted as heat

energy released to be catalysed

• Easily regenerated - can be
by the enzyme ATP hydrolase
recharged with energy
3. ATP hydrolysis can be couple to
other reactions in the cell - the
energy can be used directly to
make the coupled reaction
happen (instead of being lost as
How does ATP carry energy? heat)

4. The released phosphate can be

added to another compound
(phosphorylation) which often
makes the compound more
reactive

5. ATP can be re-synthesised in a

condensation reaction between
ADP and Pi. The enzyme ATP
synthase catalyses it during both
respiration and photosynthesis