CARBOHYDRATES

Key Terms

Monomers

3.1 BIOLOGICAL MOLECULES Polymers

Condensation reaction
MISSESTRUCH 2020
Hydrolysis reaction
Monomers and Polymers

Monomers (mono meaning one, think monobrow!)

Small, single units that act as the building blocks to create
larger molecules.

Polymers (poly meaning more than two)

Made up of many monomers, usually thousands, chemically
bonded together.

Condensation and Hydrolysis Reactions

For monomers to bond together a chemical reaction occurs; this is a condensation reaction.

Condensation reactions involve the removal of a water molecule. This removal of water from
monomers enables a chemical bond to form between the monomers.

A hydrolysis reaction is the opposite of this- hydro (water) lysis (to split). A water molecule is added
between two bonded monomers (within a dimer or polymer) to break the chemical bond.

1 MISSESTRUCH 2020
CARBOHYDRATES
Key Terms

Monosaccharides

3.1 BIOLOGICAL MOLECULES Disaccharides

Polysaccharides
MISSESTRUCH 2020
Glucose
Carbohydrates Galactose
Fructose
Carbohydrates are key biological molecules that store energy
and can provide structural support to plant cells.

Carbohydrates can be classified into three groups determined by how many units they are made of,
as seen in the flow diagram below.

Fructose

Larger carbohydrates, such as sucrose and starch, are made from monosaccharides.

The monomers of carbohydrates are known as monosaccharides and glucose, galactose and
fructose are three common examples. Monosaccharides are sugars and are soluble in water.
Their function is either to provide energy or to be a building block to create larger molecules.

All carbohydrates contain three elements: carbon, hydrogen and oxygen (CHO).
The general formula for a monosaccharide is CnH 2nOn, where n = the number of carbon atoms it
contains.

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CARBOHYDRATES
Key Terms

Monosaccharides

3.1 BIOLOGICAL MOLECULES Glucose

Isomer
MISSESTRUCH 2020
α glucose
Glucose β glucose

Glucose, C 6H12O6 , is a very important monosaccharide that can

provide energy or be polymerised to form a structural support
molecule (cellulose) or energy storage molecule (glycogen and
starch).

Glucose has two structural isomers. Isomers are

compounds that have the same formula, but the
atoms are arranged differently.

The diagram on the left shows the isomer α

glucose.

β glucose is the second isomer. There is only one difference in the structural arrangement
between these isomers. The hydrogen (H) and hydroxyl group (OH) on carbon 1 swap position.

α glucose β glucose

This small change has a significant impact on the bonding and final structure of the polymers
that they form.

3 MISSESTRUCH 2020
CARBOHYDRATES
Key Terms

Monosaccharides

3.1 BIOLOGICAL MOLECULES Disaccharides

Glycosidic Bond
MISSESTRUCH 2020
Maltose
Disaccharides
Lactose

Disaccharides are two monosaccharides bonded together by Sucrose

a glycosidic bond, that is formed by a condensation reaction.

There are three key disaccharides that you need to remember, and these are made from the three
key monosaccharides you learned.

glucose + glucose --> maltose

glucose + galactose --> lactose

glucose + fructose --> sucrose

Condensation and Hydrolysis Reactions

The diagram below demonstrates how a condensation reaction creates a disaccharide. A water
molecule is being removed (highlighted in red) from the hydroxyl group (OH) on carbon 1 and carbon
4 on the two monosaccharides. The bond that forms is known as a glycosidic bond (highlighted in
blue). This diagram shows a 1-4, glycosidic bond because it is located between carbon 1 and
carbon 4.

Disaccharides can be broken down back into monosaccharides via a hydrolysis reaction. Hydrolysis
is when a water molecule is added in to break a bond, as shown in the diagram below.

MISSESTRUCH 2020
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CARBOHYDRATES
Key Terms

Polysaccharides

3.1 BIOLOGICAL MOLECULES Condensation reaction

Energy store
MISSESTRUCH 2020
Structural support
Polysaccharides
Starch

Polysaccharides are polymers made up of many Glycosidic bonds

monosaccharides. A polysaccharide is created in the same way

as a disaccharide, via condensation reactions. There are three
key polysaccharides that you need to learn the structure and
function of: starch, glycogen and cellulose.

Starch and glycogen are both energy stores, whereas cellulose provides structural support.

Starch

Starch is found in plants, not in animal cells, and it is the major carbohydrate store. Starch is made
from the excess glucose created during photosynthesis. Glucose is used in respiration, but if more
glucose is created in photosynthesis than is needed, it is converted into the polymer starch for
storage.

Structure of starch

Starch is a polymer made up of α-glucose. These α-glucose monomers are joined together via
condensation reactions and are held in place by 1,4 and 1,6 - glycosidic bonds (The numbers refer
to which carbon atoms the bond forms between).

5
MISSESTRUCH 2020
CARBOHYDRATES
Key Terms

Starch

3.1 BIOLOGICAL MOLECULES Amylose

Amylopectin
MISSESTRUCH 2020
Glycosidic bonds
Structure of Starch
Spiral

Starch is made up of two polymers; amylose and amylopectin. Branched

Amylose is the name of the structure in starch in which the glucose monomers are all joined
together by 1,4 - glycosidic bonds. This results in a spiral-shaped polymer, see diagram below.

Amylopectin is the name given to the other structure in

starch in which the glucose monomers are joined by a
combination of 1,4 and 1,6 - glycosidic bonds. The 1,6 -
glycosidic bonds result in branches, as seen in the diagram
to the right.

Properties of Starch

Starch is insoluble due to the fact it is a large molecule. This is an advantage as it means it can
be stored within cells and not dissolve. Therefore it will not change the water potential of a cell
and nor cause osmosis to occur.

As amylose is spiral-shaped, it can be readily compacted.

As amylopectin is branched, it provides a larger surface area for enzymes to attach to.
This means that starch is readily hydrolysed back into glucose when plant cells are running low
on glucose for respiration.

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CARBOHYDRATES
Key Terms

Glycogen

3.1 BIOLOGICAL MOLECULES Glycosidic bonds

Highly branched
MISSESTRUCH 2020
Glycogen Metabolic rate
Liver
Glycogen is the major carbohydrate storage molecule found in Muscles
animal cells. The main cells glycogen is stored in are liver and
muscle cells.

Glycogen is made from the excess glucose that has been eaten and absorbed into the bloodstream.
Glucose is used in respiration, but if more glucose is eaten than the cells need for respiration it is
converted into the polymer glycogen and stored. As liver cells are responsible for removing toxins
and muscles are responsible for movement, glycogen is mainly stored in these cells to ensure they
always have access to glucose to respire and release energy.

Structure of Glycogen

Glycogen is a polymer made up of α-glucose and is very similar in structure

to amylopectin in starch. The α-glucose monomers are joined together via
condensation reactions and are held in place by 1,4 and 1,6 - glycosidic
bonds. The key difference between the structure of glycogen and starch is
that glycogen contains more 1,6 - glycosidic bonds and is, therefore, a more
branched structure.

Properties of Glycogen

Glycogen is insoluble due to the fact it is a large molecule. This is an advantage as it means it can
be stored within cells and not dissolve. Therefore it will not change the water potential of a cell
nor cause osmosis, which would otherwise cause cell lysis.

The fact that glycogen is a highly branched molecule means it has a larger surface area for
enzymes to attach. This means that it is readily hydrolysed into glucose when cells are running
low on glucose. Glycogen is even more branched than starch, therefore it is hydrolysed back into
glucose more rapidly. This is essential for animals because they have a higher metabolic rate and
therefore need more glucose. For example, they may need this glucose to provide energy to run
from a predator.
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MISSESTRUCH
CARBOHYDRATES
Key Terms

Cellulose

3.1 BIOLOGICAL MOLECULES Structural strength

β-glucose
MISSESTRUCH 2020
Cellulose Glycosidic bonds
Unbranched
Unlike starch and glycogen, the function of cellulose is to Fibril
provide structural strength in plants. Cellulose is located in
the cell wall of plants and therefore prevents cells from
bursting if they take in excess water.

Structure of Cellulose

Cellulose is the only polysaccharide that is made up of β-glucose

monomers. These monomers are joined by 1,4 - glycosidic bonds only.
For this reason, the cellulose polymer is unbranched (1-4 bonds create
straight lines, whereas 1-6 bonds create branches).

These long, straight chains of β-glucose accumulate and lie parallel to each other. The parallel
chains are then held together by many hydrogen bonds, and the sheer number of hydrogen bonds
provides strength.

This structure is called a fibril. Fibrils then align in parallel and are held in place by even more
hydrogen bonds to form a cellulose fibres.

Properties of Cellulose
Key Points:

Monomers join together by condensation reactions to make

Cellulose is insoluble due to the fact it
polymers. Polymers are hydrolysed back into monomers.
is such a large molecule. This is an
advantage as it will not change the
Monosaccharides are the monomers of carbohydrates. Glucose,
galactose and fructose are the three you need to know. Glucose water potential of a cell and affect
exists as two isomers, α-glucose and β-glucose. osmosis. Due to the large number of
hydrogen bonds in and between the
Three key disaccharides are maltose, lactose and sucrose. fibrils, cellulose is a very strong
polysaccharide.
Three key polysaccharides are starch, glycogen and cellulose.
Glycogen is for glucose storage in animals.
Starch is for glucose storage in plants.
Cellulose is for structural strength in plants.
MISSESTRUCH 2020
8
Essay Links:

Glucose could link to titles on respiration, as a key respiratory substrate

Glucose and glycogen could link to homeostasis and the control of blood glucose levels.
Glycosidic bonds and hydrogen bonds (in cellulose) could link to titles on bonding.
Monosaccharides and polysaccharides could link to titles on monomers and polymers.

8 MISSESTRUCH 2020
PROTEINS
Key Terms

Polypeptide
3.1 BIOLOGICAL MOLECULES Peptide bonds

MISSESTRUCH 2020 Amino acids

Amine group

Carboxyl group

Protein structure overview

Proteins are large polymers made up of monomers called

amino acids. These amino acids are arranged in a series of
structures to create the finished 3D protein. There are up to
four levels of structural
arrangements in a protein.

Protein polymer chains, or polypeptides, are created

on ribosomes in cells and are then further folded and modified
in the Golgi apparatus.

Monomer in proteins - Amino acid

Proteins are large polymers, made up the monomer amino acids. There are 20 different amino
acids, but you only need to learn the general structure.

The general structure consists of:

a central carbon
an amine group (NH 2)
a hydrogen atom
a carboxyl group (COOH)
the variable group (R group)

Each of the 20 different amino acids have a different R group.

Amino acids join together to make the polypeptide polymer via condensation reactions and are held
together by peptide bonds.
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 PROTEINS
Key Terms

Primary structure
3.1 BIOLOGICAL MOLECULES Sequence of amino acids

MISSESTRUCH 2020 α helix

Primary Structure
β pleated sheet

Secondary structure
The first structure that forms in the creation of a protein is the
polypeptide chain.

Amino acids

Proteins are all made up of one or more polypeptide chains folded into highly specific 3D shapes.
The primary structure is the sequence of amino acids in a polypeptide chain. This would be a one-
mark question and it is essential that you state the word ‘sequence’.

The order the amino acids are bonded in is determined by DNA. This specific order of amino acids
will alter where bonds occur and how the protein folds. Therefore, the primary structure
determines the final 3D shape and the protein's function.

There are 20 different amino acids that can form the primary structure. The polypeptide chain is
created by a series of condensation reactions occurring between amino acids. Each amino acid is
held in the polypeptide chain by peptide bonds.

Secondary Structure

The sequence of amino acids causes parts of a protein

molecule to bend into an α helix or fold into β pleated
sheets.

Hydrogen bonds form between the carboxyl groups of

one amino acid and the amine group of another and hold
the secondary structure in place.
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PROTEINS
Key Terms

Tertiary structure
3.1 BIOLOGICAL MOLECULES Hydrogen bonds

MISSESTRUCH 2020 Ionic bonds

Tertiary Structure
Disulfide bonds

Quaternary structure
The secondary structure is bent and folded to form a precise
3D shape. This unique 3D shape is held in place by hydrogen Haemoglobin

bonds, ionic bonds and sometimes disulfide bonds. Disulfide

bonds (di meaning 2) only form between the R-groups of two
amino acids that contain sulfur.

Describing the tertiary structure of a protein is a 3-mark question. The 3 marks are:
The further folding of the secondary structure
To create a unique 3D structure
Held in place by hydrogen, ionic and disulfide bonds.

Make sure you always mention the bonds involved when describing protein structures, as there are
always marks for this because without these bonds the unique shapes are not maintained.

Quaternary Structure

A protein that is made up of more than one polypeptide chain has a quaternary structure. It is still
folded into a 3D shape and held by hydrogen, ionic and disulphide bonds. Haemoglobin is an
example which is made up of 4 polypeptide chains.

In the diagram of haemoglobin, you can also see extra

molecules attached that are not part of the polypeptide
chains. Any group that is attached to a protein, but is not
made up of amino acids, is known as a prosthetic group.
The heme group, containing iron, is the prosthetic group
in haemoglobin. A protein that has a prosthetic group
can be described as a conjugated protein, which simply
means a non-protein group is added onto it.

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PROTEINS
3.1 BIOLOGICAL MOLECULES
MISSESTRUCH 2020

Key points

Proteins are large polymers made up of amino acids, held together by peptide bonds.
There are four levels of organisation; primary, secondary, tertiary and quaternary structure.
Peptide bonds hold the primary structure.
Hydrogen bonds hold the secondary structure
Hydrogen, ionic and disulfide bonds hold the tertiary structure.

Essay Links:

The primary structure can link to titles on mutations.

The tertiary structure could link to titles on transport across membranes (carrier/channel proteins).
The tertiary structure could link to titles on receptors.
The tertiary structure could link to titles on immunity (antigens and antibodies).

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 ENZYMES
Key Terms

Active site
3.1 BIOLOGICAL MOLECULES Tertiary structure

MISSESTRUCH 2020 Complementary

Enzyme Structure Activation energy

Whilst enzymes are relatively large molecules, it is only a small

part of the enzyme that attaches to a substrate to catalyse a
reaction. This site is known as the active site. The active site is
specific and unique in shape due to the specific folding and
bonding in the tertiary structure of the protein. Due to this
specific active site, enzymes can only attach to
substrates that are complementary in shape.

Protein polymer chains, or polypeptides, are created

on ribosomes in cells and are then further folded and modified in
the Golgi apparatus.

Enzyme Action

All reactions require a certain amount of energy before they occur. This is known as the activation
energy. When enzymes attach to the substrate they can lower the activation energy needed
for the reaction to occur, and therefore speed up the reaction.

13 MISSESTRUCH 2020
ENZYMES
Key Terms

Lock and key

3.1 BIOLOGICAL MOLECULES Induced fit

MISSESTRUCH 2020 Enzyme-substrate

Two models of action complex

There are two models to explain how this occurs: lock and key model and induced fit model.

Lock and Key Model

This model suggests that the enzyme is like a lock and that the substrate is like a key that
fits into it due to its complementary shape. The enzyme active site is a fixed shape and due to
random collisions, the substrate can collide and attach to the enzyme. This forms an enzyme-
substrate complex.

Once the enzyme-substrate complex has formed, the charged

groups within the active site are thought to distort the substrate
and therefore lower the activation energy.

The products are then released, and the enzyme active site is empty
and ready to be reused.

Induced Fit Model

This model suggests that the enzyme is like a glove and the substrate is like your hand; the empty
glove is not exactly complementary in shape to your hand, but when your hand enters, it enables
the glove to mould around your hand to become completely complementary. The enzyme active site
is induced or slightly changes shape, to mould around the substrate. The formation of the enzyme-
substrate complex involves the enzyme moulding around the substrate, which puts a strain on the
bonds and therefore lowers the activation energy.

The products are then removed, and

the enzyme active site returns to its
original shape.
The induced fit model is the accepted
model for how enzymes function.

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ENZYMES
Key Terms

Kinetic energy
3.1 BIOLOGICAL MOLECULES Successful collisions

MISSESTRUCH 2020 Denature

Factors Affecting Enzymes

Enzymes, which are proteins, are sensitive to certain conditions.

The following factors affect the rate of enzyme-controlled reactions:

•Temperature
•pH
•Substrate concentration
•Enzyme concentration
•Inhibitors

Temperature

If the temperature is too low, there is not enough kinetic energy for successful collisions between
the enzyme and substrate.

If the temperature is too high, enzymes denature, the active site changes shape and enzyme-
substrate complexes cannot form.

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ENZYMES
Key Terms

Amino acids
3.1 BIOLOGICAL MOLECULES Enzyme-substrate complex

MISSESTRUCH 2020 Denature

pH Saturated

Too high or too low a pH will interfere with the

charges in the amino acids in the active site.
This can break the ionic and hydrogen bonds
holding the tertiary structure in place and therefore
the active site changes shape.

Therefore the enzyme denatures and fewer

enzyme-substrate complexes form.

Different enzymes have a different optimal pH

Substrate and Enzyme Concentration

If there is insufficient substrate, then the reaction will be slower as there will be fewer collisions
between the enzyme and substrate.

If there are insufficient enzymes, then the enzyme active sites will become saturated with
substrate and unable to work any faster.

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MISSESTRUCH 2020
ENZYMES
Key Terms

Competitive inhibitor
3.1 BIOLOGICAL MOLECULES Enzyme-inhibitor complex

MISSESTRUCH 2020 Non-competitive inhibitor

Inhibitors

Competitive inhibitors are the same shape as the substrate and can bind to the active site. This
prevents the substrate from binding and the reaction occurring. If you add more substrate this will
out-compete the inhibitor, knocking them out of the active site.

Non-competitive inhibitors bind to the enzyme away from the active site (the allosteric site). This
causes the active site to permanently change shape, and therefore the substrate can no longer bind,
regardless of how much substrate is added.

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MISSESTRUCH 2020
ENZYMES
Key Terms

Competitive inhiitor
3.1 BIOLOGICAL MOLECULES Enzyme-inhibitor complex

MISSESTRUCH 2020 Denature

Inhibitor Graphs

With a high enough substrate concentration, the

competitive inhibitors are knocked out of the
active site and the rate of reaction will
therefore return to the same as with no
inhibitor.

The rate of reaction with a non-competitive

inhibitor will be lower at all substrate
concentrations.

Key points

Enzymes are tertiary structure proteins.

Enzymes catalyse specific reactions due to their uniquely shaped active site
How enzymes lower activation energy is demonstrated by the induced fit model
Enzymes are sensitive to pH and temperature.
Inhibitors, substrate and enzyme concentration affect the rate of reaction.

Essay Links:

Beyond the spec: Cyanide is a competitive inhibitor for an enzyme in respiration, which is why it is
poisonous.
Enzyme sensitivity to pH and temperature can be linked to homeostasis - thermoregulation and regulation
of pH of the blood.
Enzyme function and sensitivity to temperature can be linked to Rubisco in photosynthesis.
Lysozyme is a hydrolytic enzyme involved in phagocytosis.

18 MISSESTRUCH 2020
LIPIDS
Key Terms

Triglycerides
3.1 BIOLOGICAL MOLECULES Condensation reaction

MISSESTRUCH 2020 Ester bond

Saturated and unsaturared
Lipids

Triglycerides and phospholipids are the two lipids

you need to know the structure and function of.

Triglyceride Phospholipids
Triglycerides

Triglycerides are formed via the condensation reactions between one molecule of glycerol and
three molecules of fatty acid. Ester bonds are formed.

The R-groups are fatty acids which can be saturated or unsaturated.

Saturated fatty acids– the hydrocarbon chain has only single bonds between carbons.
Unsaturated fatty acids – the hydrocarbon chain consists of at least one double bond between
carbons

MISSESTRUCH 2020
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LIPIDS
Key Terms

Metabolic water source

3.1 BIOLOGICAL MOLECULES Hydrophobic

MISSESTRUCH 2020 Hydrophilic

Properties of Triglycerides Energy storage

Here is how the triglyceride structure results in its properties.

1. Due to the large ratio of energy-storing carbon-hydrogen bonds compared to the number of
carbon atoms; a lot of energy is stored in the molecule.
2. Due to the high ratio of hydrogen to oxygen atoms they act as a metabolic water source.
Triglycerides can release water if they are oxidised. This is essential for animals in the
desert, such as camels.
3. Triglycerides do not affect water potentials and osmosis. This is because they are large and
hydrophobic, making them insoluble in water.
4. Lipids have a relatively low mass. Therefore a lot can be stored without increasing the mass
and preventing movement.

Phospholipids

Phospholipids are made of a glycerol molecule, two fatty acid

chains and a phosphate group (attached to the glycerol).

The two fatty acids also bond to the glycerol via two condensation
reactions, resulting in two ester bonds.

The hydrophilic ‘head’ of a phospholipid can attract water as it is

charged. Due to the phosphate being charged (polar), it repels other
fats.

The fatty acid chain is not charged (non-polar). It is known as the

hydrophobic ‘tail’ and it repels water but will mix with fats.

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LIPIDS
Key Terms

Polar
3.1 BIOLOGICAL MOLECULES Phospholipid bilayer

MISSESTRUCH 2020 Plasma membrane

Phospholipids have two charged

regions, so they are polar.

In water, they are positioned so that

the heads are exposed to water and
the tails are not.

This forms a phospholipid bilayer

which makes up the plasma
membrane around cells.

Key points

Triglycerides and phospholipids are lipids.

Both molecules are formed via a condensation reaction and form ester bonds.
Fatty acids can be saturated or unsaturated, which refers to whether there are double or
single bonds between the carbon atoms.
Phospholipids have a hydrophilic head and a hydrophobic tail.

Essay Links:

Lipids form the insulating myelin sheath on neurones to enable saltatory conduction.
Lipids form the phospholipid bilayer on organelle membranes, such as mitochondria and
chloroplasts
Lipids form the membrane of vesicles, such as a phagosome.
Lipids obtained from the membranes of host cells form an envelope around viruses (i,e, HIV)

21
MISSESTRUCH 2020
BIOCHEMICAL TESTS
Key Terms

Reducing sugar
3.1 BIOLOGICAL MOLECULES Benedict's reagent

MISSESTRUCH 2020
Biochemical Test Overview

For some of the biological molecules in this topic, you need to know the experiment to test if they
are present in a substance and what a positive test result would look like.

The biological molecules you need to know the test for are:
Reducing sugars
Non-reducing sugars
Starch
Proteins
Lipids

lipids proteins starch reducing/non-reducing sugars

Reducing Sugars Test

To test for the presence of these sugars, Benedict’s reagent is added. This is a bright
blue liquid (due to it containing copper sulfate). The name reducing sugar is given to
sugars that can reduce Cu 2+ ions in Benedict’s reagent to Cu+ ions in the form of
copper (I) oxide, which forms a brick-red precipitate.

The chemical procedure for this is:

1. Add Benedict’s reagent to the sample you are testing
2. Heat
3. If a colour change of blue to yellow/green/red is observed, then this is
confirmation that a reducing sugar is present.
4. If the solution remains blue, there is no reducing sugar present.

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BIOCHEMICAL TESTS
Key Terms

Non-reducing sugar
3.1 BIOLOGICAL MOLECULES Benedict's reagent

MISSESTRUCH 2020 Acid hydrolysis

Non-reducing sugar
HCl
Sucrose is a non-reducing sugar because it cannot reduce Cu 2+, Sodium hydroxide
this is because the chemical group needed for this reduction Glycosidic bonds
reaction is involved in the glycosidic bonds between the
monosaccharides. To prove that sucrose is still a sugar, but is
just unable to reduce Cu2+ (a non-reducing sugar) the glycosidic
bond must be hydrolysed to expose the reducing group.

If a substance remained blue after the reducing sugars test, then the procedure to
test to see if it is a non-reducing sugar is as follows:

Mix sucrose with HCl and boil – this is acid hydrolysis and it breaks the glycosidic bond so that
sucrose is hydrolysed back into glucose and fructose. Hint – to get the mark you must state BOIL,
as below 100 oC there is not enough energy to break the glycosidic bond.
Cool the solution and then add sodium hydroxide to make the solution alkaline. Benedict’s
reagent only works in alkaline solutions, which is why this stage is essential. You must cool the
solution first to prevent excessive, dangerous fizzing.
Add a few drops of Benedict’s reagent and heat. If a colour change of blue to yellow/green/red
is observed, then this is confirmation that a non-reducing sugar is present.

The rustier red the precipitate that forms after a reducing or non-reducing sugar test, the higher the
concentration of sugar present. This is because more Cu 2+ has been reduced to Cu +, which forms
copper oxide otherwise known as 'rust'.

23 MISSESTRUCH 2020
 BIOCHEMICAL TESTS
Key Terms

Starch
3.1 BIOLOGICAL MOLECULES Iodine

MISSESTRUCH 2020 Protein

Starch
Biuret reagent

The presence of starch can be Lipids

confirmed by adding a few drops of Ethanol

iodine. Iodine is orange/brown in Distilled water

colour when no starch is present, White emulsion

but it turns blue/black if starch is
present.

Protein

To test for proteins you add biuret reagent (tip - do not confuse this with a
burette! It is pronounced Bi-u-ret).

Biuret reagent is blue, but it will turn purple when added to a protein.

Lipids

To test for lipids, your sample must first be dissolved in ethanol. This is achieved
by shaking the sample you are testing in ethanol. Once the sample is dissolved,
add distilled water and shake again. If lipids are present, you will then observe a
white emulsion.

Key points

For each test, you must know the name of the chemical reagent added,
whether it needs to be heated and what the positive test observation looks
like.
Benedict's reagent must be heated for the reaction to occur.
For acid hydrolysis of non-reducing sugars, the acid must be boiled.
To test for lipids, you must first dissolve in ethanol and after this, you add
and shake in distilled water.
24 MISSESTRUCH 2020
DNA & RNA
Key Terms

Deoxyribonucleic acid
3.1 BIOLOGICAL MOLECULES Nucleotide

MISSESTRUCH 2020 Nitrogenous base

DNA Structure
Phosphate group

Double helix
Deoxyribonucleic Acid (DNA) codes for the sequence of amino
acids in the primary structure of a protein, which in turn
determines the final 3D structure and function of a
protein.

It is essential that cells contain a copy of this genetic code and

that it can be passed to new cells without being damaged.

The DNA polymer is a double helix shape.

DNA Nucleotide

The monomer that makes up DNA is called a nucleotide. It is made up of deoxyribose (a

pentose sugar), a nitrogenous base and one phosphate group.

The nitrogenous base can either be guanine, cytosine, adenine and thymine.

Deoxyribose

25 MISSESTRUCH 2020
DNA & RNA
Key Terms

Polynucleotide
3.1 BIOLOGICAL MOLECULES Condensation reaction

MISSESTRUCH 2020 Phosphodiester bond

Sugar-phosphate backbone
Polynucleotides
Hydrogen bonds

The polymer of these nucleotides is called a polynucleotide. Complementary base pairs

It is created via condensation reactions between the deoxyribose

sugar and the phosphate group, creating a phosphodiester bond.
Phosphodiester bonds are strong covalent bonds, and
therefore help ensure that the genetic code is not broken down.

The polynucleotide has a sugar-phosphate ‘backbone’. This

describes the strong covalent bonds between the sugar and
phosphate groups that hold the polymer together.

The DNA polymer occurs in pairs, and these pairs are joined together by hydrogen bonds between
the bases. This is how the double helix structure is created, as the two chains twist.

Hydrogen bonds can only form between complementary base pairs. This is the term given to the
fact that the base cytosine can only form hydrogen bonds with guanine and that adenine can
only bond with thymine.

Adenine and thymine form 2 hydrogen bonds,

whereas cytosine and guanine can form 3
hydrogen bonds.

This complementary base pairing is important to

help maintain the order of the genetic code when
DNA replicates, therefore reducing the chance of
mutations.

26 MISSESTRUCH 2020
DNA & RNA
Key Terms

Ribose
3.1 BIOLOGICAL MOLECULES Uracil

MISSESTRUCH 2020 Single-stranded

How the DNA Structure Links to its Function mRNA

tRNA
Stable structure due to the sugar-phosphate backbone
rRNA
(covalent bonds) and the double helix to prevent damage.
Double-stranded so replication can occur using one strand as a template.
Weak hydrogen bonds for easy separation of the two strands in a double helix during
replication.
Large molecule to carry lots of genetic information.
Complementary base pairing allows identical copies to be made.

RNA

RNA is a polymer of a nucleotide formed of ribose, a nitrogenous base and a phosphate group.
The nitrogenous bases in RNA are adenine, guanine, cytosine and uracil.
RNA has the base uracil instead of thymine. In comparison to the DNA polymer, the RNA polymer
is a relatively short polynucleotide chain and it is single-stranded.

Ribose

The function of RNA is to copy and transfer the genetic code from DNA in the nucleus to the
ribosomes. Some RNA is also combined with proteins to create ribosomes.

There are three types of RNA;

mRNA
tRNA
rRNA
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DNA & RNA
Key Terms

Single-stranded
3.1 BIOLOGICAL MOLECULES Short-lived

MISSESTRUCH 2020 Codon

Messenger RNA (mRNA)

mRNA is a copy of a gene from DNA.

mRNA is created in the nucleus and it then leaves the nucleus to carry the copy of the genetic code
of one gene to a ribosome in the cytoplasm.

DNA is too large to leave the nucleus and would be at risk of being damaged by enzymes,
therefore destroying the genetic code permanently. mRNA is much shorter because it is only the
length of one gene, and can therefore leave the nucleus as it is small enough to fit through the
nuclear pores.

mRNA is short-lived as it is only needed temporarily to help create a protein, therefore by the
time any enzymes could break it down, it would have already carried out its function.

mRNA is single-stranded and every 3 bases in the sequence code for a specific amino acid; these
three bases are therefore called codons.

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DNA & RNA
Key Terms

Single-stranded
3.1 BIOLOGICAL MOLECULES Cloverleaf shape

MISSESTRUCH 2020 Anticodon

Transfer RNA (tRNA)

tRNA is found only in the cytoplasm.

It is single-stranded but folded to create a shape

that looks like a cloverleaf shape. This cloverleaf
shape is held in place by hydrogen bonds.

The function of tRNA is to attach to one of the 20

amino acids and transfer this amino acid to
the ribosome to create the polypeptide chain.

Specific amino acids attach to specific tRNA

molecules and this is determined by 3 bases found
on the tRNA which are complementary to the 3
bases on mRNA.

These are called the anticodon because they are

complementary to the codon on mRNA.

Ribosomal RNA (rRNA)

rRNA is the type of RNA that makes up the bulk of ribosomes. The rest of a ribosome is made of
protein.

80S
ribosome

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DNA & RNA
3.1 BIOLOGICAL MOLECULES
MISSESTRUCH 2020
DNA compared to RNA

Differences between the DNA and RNA monomer:

DNA contains the base thymine, whereas RNA contains uracil instead.
DNA contains the pentose sugar deoxyribose, whereas RNA contains the pentose sugar ribose.

Differences between the polymers:

DNA is much larger because it contains approximately 23,000 genes (the entire genome),
whereas RNA is much shorter because it is only the length of one gene.
DNA is double-stranded, whereas RNA is single-stranded.

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DNA & RNA
3.1 BIOLOGICAL MOLECULES
MISSESTRUCH 2020

Key Points

DNA and RNA are both polymers made up of nucleotide monomers.

The polymers are made via condensation reactions and phosphodiester bonds form between
the nucleotides.
There are three types of RNA: mRNA, tRNA and rRNA.
Hydrogen bonds form between the two bases on different chains on DNA and on RNA where
the chain folds.
When comparing the differences, always have the comparison within the same sentence e.g
DNA has thymine whereas RNA has uracil.
Read comparison questions carefully, are you being asked to compare the monomers or
polymers?

Essay Links:

The structure of DNA can link to the cell cycle (meiosis and mitosis) and DNA technology.
The function of DNA can link to inheritance, natural selection and evolution.
The importance of DNA can link to mutations and cancer.
RNA structure and function can link to protein synthesis.

31 MISSESTRUCH 2020
DNA REPLICATION
Key Terms

Semi-conservative
3.1 BIOLOGICAL MOLECULES Complementary base pairs

MISSESTRUCH 2020 DNA helicase

DNA polymerase
Before cells divide (by mitosis or meiosis) all the DNA must
replicate to provide a copy for the new cell.

The process of DNA replication is semi-conservative replication (in

the daughter DNA, one strand is from the parental DNA and one
strand is newly synthesised).

This process relies on the

complementary base pairs
(cytosine + guanine and
thymine + adenine) and
involves the enzymes DNA
helicase and DNA
polymerase.

There are four key stages to semi-conservative DNA replication.

Step 1:

DNA helicase breaks the hydrogen bonds between the

complementary base pairs between the two stands within a
double helix.

This causes the DNA double helix to unwind.

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DNA REPLICATION
Key Terms

Template
3.1 BIOLOGICAL MOLECULES Complementary base pairs

MISSESTRUCH 2020 DNA helicase

Step 2: DNA polymerase
Phosphodiester bond
Each of the separated parental DNA strands acts as a
template.

Free-floating DNA nucleotides within the nucleus are

attracted to their complementary base pairs on the
template strands of the parental DNA.

Step 3:

The adjacent nucleotides are joined together (to form the

phosphodiester bond) by a condensation reaction.

DNA polymerase catalyses the joining together of adjacent

nucleotides.

Step 4

The two sets of daughter DNA (the name given

to the new DNA molecules) contain one strand
of the parental (original) DNA and one newly
synthesised strand.

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DNA REPLICATION
3.1 BIOLOGICAL MOLECULES
MISSESTRUCH 2020

Key points

DNA replication is semi-conservative.

DNA helicase breaks hydrogen bonds between bases to unwind the double helix.
Free-floating DNA nucleotides in the nucleus are attracted to their complementary bases
exposed on the template strands.
DNA polymerase joins together adjacent nucleotides to make the new strand via condensation
reactions

Essay Links:

DNA replication can link to the cell cycle (meiosis and mitosis) and DNA technology.
DNA replication is when gene mutations occur which can lead to new phenotypes, therefore
natural selection and evolution. Mutations can also result in cancer.

34 MISSESTRUCH 2020
WATER
Key Terms

Polar
3.1 BIOLOGICAL MOLECULES Hydrogen bonds

MISSESTRUCH 2020 Metabolite

The Structure of Water
Solvent

High specific heat capacity

Water is an incredibly important biological
molecule, which is why about 60-70% of your body Strong cohesion
is water. Large latent heat of vaporisation

Water is a polar molecule. Water has an unevenly

distributed charge due to the fact that the oxygen
atom is slightly negative, and the hydrogen atoms
are slightly positive. The delta ( δ ) symbol
indicates a slightly positive/negative on the
diagram.

Five Key Properties of Water

Hydrogen bonds form between different water molecules between the oxygen and a hydrogen atom.
The formation of these hydrogen bonds and the fact that water is dipolar results in 5 key properties of
water:

1. It is a metabolite (e.g. in condensation and hydrolysis reactions).

2. An important solvent in reactions.
3. Has a high heat capacity, and it buffers temperature.
4. Has a large latent heat of vaporisation, providing a cooling effect with loss of water through
evaporation.
5. Has strong cohesion between water molecules; this supports water columns and provides
surface tension.

35 MISSESTRUCH 2020
WATER
Key Terms

Metabolite
3.1 BIOLOGICAL MOLECULES Hydrolysis

MISSESTRUCH 2020 Polar

Metabolite
Solvent

Hydrophobic
Water is involved in many reactions, such as photosynthesis,
hydrolysis, and condensation reactions. Hydrophilic

This is one reason why it is essential that approximately

90% of the plasma in the blood and the cytoplasm in cells is
largely composed of water.

Solvent

Water is a good solvent, meaning many substances dissolve in

it. Polar (or charged) molecules dissolve readily in water due to
the fact water is polar. The slight positive charge on hydrogen
atoms will attract any negative ions in solutes and the slight
negative charge on the oxygen atoms of water will attract any
positive ions in solutes. These polar molecules are often
described as hydrophilic, meaning they are attracted to water.

Non-polar molecules, such as lipids, cannot dissolve in water and are therefore described as
hydrophobic- they are repelled by water.

The fact that so many essential polar substances dissolve in water enables them to be transported
easily around animals and plants through blood or xylem.

36 MISSESTRUCH 2020
WATER
Key Terms

High specific heat capacity

3.1 BIOLOGICAL MOLECULES Hydrogen bonds

MISSESTRUCH 2020 Denature

High Specific Heat Capacity
Evaporate

Cooling effect
This means that a lot of energy is required to raise the
temperature of the water. This is because some of the heat Sweating
energy is used to break the hydrogen bonds between water
molecules.

This is useful to organisms as it means the temperature of the water remains relatively stable, even if
the surrounding temperature fluctuates significantly. Therefore, the internal temperatures of plants
and animals should remain relatively constant despite the outside temperature, due to the fact a large
proportion of the organism is water.

This is important so that enzymes do not

denature or reduce activity with temperature
fluctuations. Finally, this provides a stable
environment, in terms of temperature, for
aquatic organisms.

Large Latent Heat of Vaporisation

This means that a lot of energy is required to convert water in its liquid state to a gaseous state.
This is due to the hydrogen bonds, as energy is needed to break the hydrogen bonds between water
molecules to turn it into a gas.
This is advantageous to organisms as it means that water
provides a significant cooling effect.

For example, when humans sweat they release water onto their
skin. Large amounts of heat energy from the skin is transferred
to the water during evaporation and this provides a cooling
effect.

37 MISSESTRUCH 2020
WATER
Key Terms

Cohesion
3.1 BIOLOGICAL MOLECULES Surface tension

MISSESTRUCH 2020 Continuous water column

Strong Cohesion

Cohesion is the term used to describe water molecules ‘sticking’

together by hydrogen bonds.
Due to water molecules sticking together, when water moves up
the xylem in plants due to transpiration it is as a continuous
column of water. This is advantageous as it is easier to draw up a
column rather than individual molecules.

Cohesion also provides surface tension to water. This enables

small invertebrates to move and live on the surface, providing them
with a habitat away from predators within the water.

Key points

Water is a polar molecule

Hydrogen bonds form between water molecules.
The polar nature and hydrogen bonds result in 5 key properties: metabolite, it is a solvent,
strong cohesion, high specific heat capacity and a large latent heat of vaporisation.

Essay Links:

The strong cohesion links to transpiration in plants.

Water is a good solvent links to mass transport in plants and animals.
Water as a metabolite links to many key reactions, such as photosynthesis and respiration.

38 MISSESTRUCH 2020
ATP & INORGANIC IONS Key Terms

3.1 BIOLOGICAL MOLECULES Immediate energy source

ATP synthase

ATP MISSESTRUCH 2020 ATP hydrolase

Inorganic phosphate
ATP, or Adenosine Triphosphate, is an immediate source of
energy for biological processes. Metabolic reactions in cells must
have a constant, steady supply of ATP. ATP contains three
phosphate ions that play a significant role in energy transfer. This
biological molecule is essential to metabolism, which is all the
chemical reactions that take place in a cell.

ATP is comprised of:

Adenine is a nitrogenous base (meaning a base that contains
nitrogen)
Ribose (a pentose sugar)
Three inorganic phosphate groups.

The phosphate groups are described as being inorganic because they do not contain any carbon
atoms. For this reason in chemical reactions the symbol to represent this is a P for phosphate and i
for inorganic -Pi

ATP is made during respiration from ADP, adenosine diphosphate, by the addition of an inorganic
phosphate via a condensation reaction which uses the enzyme ATP synthase.

ATP can be hydrolysed into ADP + Pi using the enzyme ATP hydrolase.

ATP + water --> ADP +Pi (energy)

By breaking one of the bonds between the inorganic phosphate groups in a hydrolysis reaction, a
small amount of energy is released to the surroundings, which can be used in chemical reactions.

Therefore, ATP is an immediate energy source as only one bond has to be hydrolysed to release
energy.

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ATP & INORGANIC IONS Key Terms

3.1 BIOLOGICAL MOLECULES Immediate energy source

Phosphorylation

MISSESTRUCH 2020 Soluble

Phosphorylation Hydrolysis

ATP can also transfer energy to different compounds. The inorganic phosphate released during the
hydrolysis of ATP can be bonded onto different compounds to make them more reactive.

This is known as phosphorylation, and this happens to glucose at the start of respiration to make it
more reactive.

There are five key properties of ATP that make it a suitable immediate source of energy. In exam
questions, the properties of ATP and glucose can be compared to emphasise the importance of ATP
as the immediate source of energy for cells rather than glucose. This is explained and
demonstrated in the five points below.

1. ATP releases energy in small, manageable amounts so no energy is wasted. This means that
cells do not overheat from wasted heat energy and cells are less likely to run out of
resources. In comparison to glucose, this would release large amounts of energy that could
result in wasted energy.
2. It is small and soluble so it is easily transported around the cell. ATP can move around the
cytoplasm with ease to provide energy for chemical reactions within the cell. This is a property
ATP has in common with glucose.
3. Only one bond is hydrolysed to release energy, which is why energy release is immediate.
Glucose would need several bonds to be broken down to release all its energy.
4. It can transfer energy to another molecule by transferring one of its phosphate groups. ATP
can enable phosphorylation, making other compounds more reactive. Glucose cannot do this,
as it does not contain phosphate groups.
5. ATP can’t pass out of the cell; the cell always has an immediate supply of energy. ATP cannot
leave the cell, whereas glucose can. This means that all cells have a constant supply of ATP (or
ADP + Pi), but a cell can run out of glucose.
40 MISSESTRUCH 2020
ATP & INORGANIC IONS Key Terms

3.1 BIOLOGICAL MOLECULES Dissolve

Solutions

MISSESTRUCH 2020
Inorganic Ions

Inorganic ions dissolve to form solutions found within the cytoplasm of cells and other body fluids.
Some inorganic ions are required in high concentrations, whereas others are required in very low
concentrations. Each inorganic ion performs a different function and this is due to their different
properties.

You need to know the role of:

Hydrogen Ions – how they determine pH (linked to enzymes)
Iron ions – a compound of haemoglobin (linked to the transport of oxygen)
Sodium ions – involved in co-transport (linked to the absorption of glucose and amino acids in the
ileum)
Phosphate ions – as a component of DNA and ATP (linked to nucleotides and nucleotide derivatives)

Key points

ATP is a nucleotide derivative, made of adenine, ribose and 3 phosphate groups.

ATP is the immediate source of energy for a cell.
Phosphorylation is the addition of an inorganic phosphate to a molecule, transferring energy
to that molecule.
Inorganic ions dissolve in solutions and perform different functions.

Essay Links:

Beyond the spec: Cholera release toxins affecting chloride ion channels. This lowers the water potential
of the small intestine's lumen causing diarrhoea.
Links to respiration, as glucose is phosphorylated in glycolysis.
Links to respiration as ADP is phosphorylated to ATP in oxidative phosphorylation.
Links to muscle contraction, as ATP is required in the sliding filament theory.
Links to active transport (resting potential, co-transport in the phloem, absorption of glucose) which
requires ATP.

MISSESTRUCH 2020
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Image Credits:
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https://commons.wikimedia.org/wiki/File:Carbonic_anhydrase_reaction_in_tissue.svg
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https://commons.wikimedia.org/wiki/File:220_Triglycerides-01.jpg
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https://commons.wikimedia.org/wiki/File:Figure_05_01_02.jpg
https://commons.wikimedia.org/wiki/File:0302_Phospholipid_Bilayer.jpg

https://commons.wikimedia.org/wiki/File:1904_Hemoglobin.jpg
https://commons.wikimedia.org/wiki/File:Figure_03_04_09.jpg

https://commons.wikimedia.org/wiki/File:DNA_chemical_structure.svg
https://www.flickr.com/photos/gemmerich/7445337412
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https://www.needpix.com/photo/89414/nucleotide-dna-pyrimidine-rna-biology-chemical-chemistry-science
https://commons.wikimedia.org/wiki/File:OSC_Microbio_10_03_tRNA.jpg
https://commons.wikimedia.org/wiki/File:Process_of_transcription_(13080846733).jpg
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https://commons.wikimedia.org/wiki/File:OSC_Microbio_03_03_Ribosome.jpg
Image Credits:
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https://www.flickr.com/photos/gails_pictures/6878227730
Image Credits:
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