Carbohydrates contain 3 elements:

1. Carbon (C)
2. Hydrogen (H)
3. Oxygen (O)

Carbohydrates are found in one of three forms:

1. Monosaccharides
2. Disaccharides (both sugars)
3. Polysaccharides

Monosaccharides

General formula:.

(CH2O)n where n is a number between 3 and 9. They are classified according to the number of carbon
atoms. The monosaccharides you will have to know fall into these categories:

C = 3 = triose

C = 4 = tetrose

C = 5 = pentose

C = 6 = hexose

Trioses: (e.g. glyceraldehydes), intermediates in respiration and photosynthesis.

Tetroses: rare.

Pentoses: (e.g. ribose, ribulose), used in the synthesis of nucleic

acids (RNA and DNA), co-enzymes (NAD, NADP, FAD) and ATP.

Hexoses: (e.g. glucose, fructose), used as a source of energy in

respiration and as building blocks for larger molecules.

All but one carbon atom have an alcohol (OH) group attached. The remaining
carbon atom has an aldehyde or ketone group attached.
Chain form:

Ring form:

Due to the bond angles between the carbon atoms, it is possible for pentoses and hexoses to form stable
ring structures. The carbon atoms are numbered 1 to 5 in pentoses and 1 to 6 in hexoses.

Depending on the orientation of the OH group on carbon 1, the monosaccharide can have either α or β
configurations.

Disaccharides and glycosidic bonds

These are formed when two monosaccharides are condensed together. One monosaccharide loses an H
atom from carbon atom number 1 and the other loses an OH group from carbon 4 to form the bond.

The reaction, which is called a condensation reaction, involves the loss of water (H2O) and the formation
of an 1,4-glycosidic bond. Depending on the monosaccharides used, this can be an α-1,4-glycosidic bond
or a β-1,4-glycosidic bond.
The reverse of this reaction, the formation of two monosaccharides from one disaccharide, is called
a hydrolysis reaction and requires one water molecule to supply the H and OH to the sugars formed.

Examples of Disaccharides

Sucrose: glucose + fructose,

Lactose: glucose + galactose,

Maltose: glucose + glucose.

Maltose: glucose + glucose.

Sucrose is used in many plants for transporting food reserves, often from the leaves to other parts of the
plant. Lactose is the sugar found in the milk of mammals and maltose is the first product of starch
digestion and is further broken down to glucose before absorption in the human gut.
 Polysaccharides

Relationship of structure
Polysaccharide: Function: Structure:
to function:

Made of 2 polymers - amylose and

amylopectin.
Insoluble therefore good
for storage.
Amylose: a polymer of glucoses joined
by α-1,4-glycosidic bonds. Forms a helix
Helix is compact.
Main storage with 6 glucose molecules per turn and
Starch polysaccharide in about 300 per helix.
The branches mean that
plants.
the compound can easily
Amylopectin: a polymer of glucoses
hydrolysed to release the
joined by α-1,4-glycosidic bonds but
glucose monomers.
with branches of α-1,6-glycosidic bonds.
This causes the molecule to be branched
rather than helical

The number and length of

Main storage
Similar to amylopectin but with many the branches means that
Glycogen polysaccharide in
more branches which are also shorter. it is extremely compact
animals and fungi
and very fast hydrolysis.
Adjacent chains of long, unbranched The microfibrils are strong
Main structural
polymers of glucose joined by β-1,4- and so are structurally
Cellulose constituent of plant
glycosidic bonds hydrogen bond with important in plant cell
cell walls
each other to form microfibrils. walls.

Functions of carbohydrates

1. Substrate for respiration (glucose is essential for cardiac tissues).

2. Intermediate in respiration (e.g. glyceraldehydes).
3. Energy stores (e.g. starch, glycogen).
4. Structural (e.g. cellulose, chitin in arthropod exoskeletons and fungal walls).
5. Transport (e.g. sucrose is transported in the phloem of a plant).
6. Recognition of molecules outside a cell (e.g. attached to proteins or lipids on cell surface membrane).
Lipids are made up of the elements carbon, hydrogen and oxygen but in different proportions to
carbohydrates. The most common type of lipid is the triglyceride.

Lipids can exist as fats, oils and waxes. Fats and oils are very similar in structure (triglycerides).

At room temperature, fats are solids and oils are liquids. Fats are of animal origin, while oils tend to be
found in plants.

Waxes have a different structure (esters of fatty acids with long chain alcohols) and can be found in both
animals and plants.

Triglycerides

These are made up of 3 fatty acid chains attached to a glycerol molecule.

Fatty acids are chains of carbon atoms, the terminal one having an OOH group attached making a
carboxylic group (COOH). The length of the chain is usually between 14 and 22 carbons long (most
commonly 16-18).

Three of these chains become attached to a glycerol molecule which has 3 OH groups attached to its 3
carbons. This is called a condensation reaction because 3 water molecules are formed from 3 OH groups
from the fatty acids chains and 3 H atoms from the glycerol. The bond between the fatty acid chain and
the glycerol is called an ester linkage.

The 3 fatty acids may be identical or they may have

different structures.

In the fatty acid chains the carbon atoms may have single bonds between them making the
lipid saturated. These are usually solid at room temperature and are called fats.

If one or more bonds between the carbon atoms are double bonds, the lipid is unsaturated. These are
usually liquid at room temperature and are called oils.
 Functions of lipids

1. Storage - lipids are non-polar and so are insoluble in water.

2. High-energy store - they have a high proportion of H atoms relative to O atoms and so yield more energy
than the same mass of carbohydrate.
3. Production of metabolic water - some water is produced as a final result of respiration.
4. Thermal insulation - fat conducts heat very slowly so having a layer under the skin keeps metabolic heat
in.
5. Electrical insulation - the myelin sheath around axons prevents ion leakage.
6. Waterproofing - waxy cuticles are useful, for example, to prevent excess evaporation from the surface of
a leaf.
7. Hormone production - steroid hormones. Oestrogen requires lipids for its formation, as do other
substances such as plant growth hormones.
8. Buoyancy - as lipids float on water, they can have a role in maintaining buoyancy in organisms.

Phospholipids

A phosphate-base group replaces one fatty acid chain. It makes this part of the molecule (the head)
soluble in water whilst the fatty acid chains remain insoluble in water.

Due to this arrangement, phospholipids form bilayers (the main component of cell and organelle
membranes).

Different proteins can appear very different and perform

diverse functions (e.g. the water-soluble antibodies involved in
the immune system and the water-insoluble keratin of hair,
hooves and feathers). Despite this, each one is made up
of amino acid subunits.There about 20 different amino acids
that all have a similar chemical structure but behave in very
different ways because they have different side groups.
Hence, stringing them together in different combinations
produces very different proteins.

Each amino acid has an amino group (NH2) and a carboxylic

acid group (COOH). The R group is a different molecule in
different amino acids which can make them neutral, acidic,
alkaline, aromatic (has a ring structure) or sulphur-containing.

When 2 amino acids are joined together (condensation) the

amino group from one and the acid group from another form
a bond, producing one molecule of water. The bond formed is
called a peptide bond.

Hydrolysis is the opposite of condensation and is the breaking

of a peptide bond using a molecule of water.
Primary structure of proteins

Due to the bonding and the shape and chemical nature of different amino acids, the shape of a whole
chain of amino acids (a polypeptide or protein) is specific.

This will affect the properties of the protein, just as the type of a necklace depends on the type of beads
and how they are strung together. Therefore, the primary structure depends on the order and number of
amino acids in a particular protein.

For example:Haemoglobin is made up of 4 polypeptide chains, 2α chains and 2β chains, each with a
haem group attached. There are 146 amino acids in each chain. If just one of these is wrong, serious
problems can arise (e.g. sickle cell anaemia). The red blood cells become distorted, the amount of
oxygen they can carry is reduced and blood capillaries can be blocked, leading to acute pains
called crises.

Secondary structure of proteins

This is the basic shape that the chain of amino acids takes
on. The 2 most common structures are the α-helix and the β-
pleated sheet.

This has a regular coiled structure like a spring, with the R

groups pointing towards the outside of the helix. Hydrogen
(H) bonds are relatively weak but because there are so many,
the total binding effect is strong and stable. The helix is
flexible and elastic.

This is composed of 'side by side' chains connected by H

bonds. All the peptide linkages are involved in inter-chain H
bonding so the structure is very stable.

Tertiary structure of proteins

This is the overall 3-D structure of the protein.

The shape of the protein is held together by H bonds between some of

the R groups (side chains) and ionic bonds between positively and
negatively charged side chains. These are weak interactions, but
together they help give the protein a stable shape. The protein may be
reinforced by strong covalent bonds called disulphide bridges which
form between two amino acids with sulphur groups on their side
chains.

These interactions may be electrostatic attractions between charged

groups e.g. NH3+ and O-or van der Waal's forces.
 Fibrous proteins are made of long molecules arranged to form fibres (e.g. in keratin). Several helices may
be wound around each other to form very strong fibres. Collagen is another fibrous protein, which has a
greater tensile strength than steel because it consists of three polypeptide chains coiled round each
other in a triple helix. We are largely held together by collagen as it is found in bones, cartilage, tendons
and ligaments.

Globular proteins are made of chains folded into a compact structure. One of the most important classes
are the enzymes. Although these folds are less regular than in a helix, they are highly specific and a
particular protein will always be folded in the same way. If the structure is disrupted, the protein ceases
to function properly and is said to be denatured. An example is insulin, a hormone produced by the
pancreas and involved in blood sugar regulation.

A globular protein based mostly on an α-helix is haemoglobin.

A globular protein based mostly on a β-pleated sheet is the immunoglobulin antibody molecule.

Quaternary structure of proteins

If a protein is made up of several polypeptide chains, the way they are arranged is called the quaternary
structure. Again, each protein formed has a precise and specific shape (e.g. haemoglobin)

Prosthetic groups

The majority of proteins are assisted in their functions by a prosthetic group. This may be a simple metal
ion such as zinc in the enzyme carboxypeptidase, or it may be a complex organic molecule, such as the
haem-group in haemoglobin.

Functions of proteins

1. Virtually all enzymes are proteins.

2. Structural: e.g. collagen and elastin in connective tissue, keratin in skin, hair and nails.
3. Contractile proteins: actin and myosin in muscles allow contraction and therefore movement.
4. Hormones: many hormones have a protein structure (e.g. insulin, glucagon, growth hormone).
5. Transport: for example, haemoglobin facilitates the transport of oxygen around the body, a type of
albumin in the blood transports fatty acids.
6. Transport into and out of cells: carrier and channel proteins in the cell membrane regulate movement
across it.
7. Defence: immunoglobulins (antibodies) protect the body against foreign invaders; fibrinogen in the
blood is vital for the clotting process.

The majority of the reactions that occur in living organisms are enzyme-controlled. Without them, the
rate of the reactions would be so slow as to cause serious, if not fatal, damage. Without enzymes toxins
would soon build up and the supply of respiratory substrate would decrease.

Enzymes are proteins and thus have a specific shape. They are therefore specific in the reactions that
they catalyse - one enzyme will react with molecules of one substrate.
The site of the reaction occurs in an area on the surface of the protein called the active site. Since the
active site for all molecules of one enzyme will be made up of the same arrangement of amino acids, it
has a highly specific shape.

Generally, there is only one active site on each enzyme molecule and only one type of substrate
molecule will fit into it.

Chymotrypsin and trypsin both catalyse the hydrolysis of peptide bonds but due to their shapes, the
active site of chymotrypsin only splits bonds after an aromatic amino acid (one containing a ring of
atoms) whereas trypsin only splits bonds after a basic or straight chain amino acid.

This specificity leads to the lock and key hypothesis.

However, it has been discovered that competitors for an active site (similar in shape to the substrate)
could fit even though they are larger than the substrate. This means that the substrate and active site
are a little flexible.

This has led to the induced fit model...

Induced fit model

When the enzyme and substrate form a complex, structural changes occur so that the active site fits
precisely around the substrate (the substrate induces the active site to change shape).

The reaction will take place and the product, being a different shape to the substrate, moves away from
the active site. The active site then returns to its original shape.

Enzyme controlled reactions

Reactions proceed because the products have less energy than the substrates.

However, most substrates require an input of energy to get the reaction going, (the reaction is not
spontaneous).

The energy required to initiate the reaction is called the activation energy.
 When the substrate(s) react, they need to form a complex called the transition state before the reaction
actually occurs. This transition state has a higher energy level than either the substrates or the product.

Outside the body, high temperatures often supply the energy required for a reaction. This clearly would
be hazardous inside the body though! Fortunately we have enzymes that provide an alternative way with
a different transition state and lower activation energy.

The rate of the reaction without any external means of providing the activation energy continues at a
much faster rate with an appropriate enzyme than without it. The maximum rate that any reaction can
proceed at will depend, among other things, upon the number of enzyme molecules and therefore the
number of active sits available.

Factors affecting the rate of reaction

1. Temperature: enzymes work best at an optimum temperature.

Below this, an increase in temperature provides more kinetic energy to the molecules involved. The
numbers of collisions between enzyme and substrate will increase so the rate will too.

Above the optimum temperature, and the enzymes are denatured. Bonds holding the structure together
will be broken and the active site loses its shape and will no longer work.
2. pH: as with temperature, enzymes have an optimum pH. If the pH changes much from the optimum, the
chemical nature of the amino acids can change.

This may result in a change in the bonds and so the tertiary structure may break down. The active site
will be disrupted and the enzyme will be denatured.

3. Enzyme concentration: at low enzyme concentration there is great competition for the active sites and
the rate of reaction is low. As the enzyme concentration increases, there are more active sites and the
reaction can proceed at a faster rate.

Eventually, increasing the enzyme concentration beyond a certain point has no effect because the
substrate concentration becomes the limiting factor.

4. Substrate concentration: at a low substrate concentration there are many active sites that are not
occupied. This means that the reaction rate is low.

When more substrate molecules are added, more enzyme-substrate complexes can be formed. As there
are more active sites, and the rate of reaction increases.

Eventually, increasing the substrate concentration yet further will have no effect. The active sites will be
saturated so no more enzyme-substrate complexes can be formed.
 Cofactors

Most enzymes require additional help from cofactors, of which there are 2 main types:

1. Coenzymes - these are organic compounds, often containing a vitamin molecule as part of their
structure.

Coenzymes are not permanently bound to the enzyme but may be temporarily and loosely bound for the
duration of the reaction and then move away once it is completed. For example NAD, which transfers
hydrogen away from one molecule in a dehydrogenase reaction and takes it to another molecule (see
the Respiration Learn-it).

2. Metal ions - most speed up the formation of the enzyme-substrate complex by altering the charge in the
active site e.g. amylase requires chloride ions, catalase requires iron.

Inhibitors

Inhibitors slow down the rate of a reaction. Sometimes this is a necessary way of making sure that the
reaction does not proceed too fast, at other times, it is undesirable.

Reversible inhibitors:

Competitive reversible inhibitors: these molecules have a similar structure to the actual substrate and
so will bind temporarily with the active site. The rate of reaction will be closer to the maximum when
there is more 'real' substrate, (e.g. arabinose competes with glucose for the active sites on glucose
oxidase enzyme).

Non-competitive reversible inhibitors: these molecules are not necessarily anything like the substrate in
shape. They bind with the enzyme, but not at the active site. This binding does change the shape of the
enzyme though, so the reaction rate decreases.
Irreversible inhibitors:

These molecules bind permanently with the enzyme molecule and so effectively reduce the enzyme
concentration, thus limiting the rate of reaction, for example, cyanide irreversibly inhibits the enzyme
cytochrome oxidase found in the electron transport chain used in respiration. If this cannot be used,
death will occur.

Industrial uses of enzymes

Many of the reactions catalysed by enzymes have commercial uses. Previously, these reactions were
made to happen without enzymes by using heat and/or strong acids but enzymes offer the following
advantages:

They are specific in their action and are therefore less likely to produce unwanted by-products.

They are biodegradable and so cause less environmental pollution.

They work in mild conditions i.e. low temperatures, neutral pH and normal atmospheric pressure, and
are therefore energy saving.

However, the last advantage can also be seen as a disadvantage as their conditions must be stringently
controlled or the enzyme may become denatured.

To be effective in a production process the enzyme molecule must be brought into maximum contact
with the substrate molecules. The solutions can be mixed in suitable concentrations or immobilisation of
the enzyme may be used. This involves attaching the enzyme to an inert surface such as plastic beads
and then bringing the surface into contact with a solution of the substrate. Immobilisation has the
advantage that the enzyme molecules can be used over and over again, with the result that a lot of
product can be made from a relatively small amount of enzyme. An example of the use of
immobilization is in the use of lactase. This enzyme hydrolyses lactose (milk sugar), into glucose and
galactose.

Examples of the industrial uses of enzymes

Perhaps the best known use is that of protease in biological washing powders.
This enzyme helps to break down protein stains such as blood at lower washing
machine temperatures. This means they save energy and are gentler on clothes.
Some people are allergic to biological washing powders but this may be overcome
by encapsulating the enzymes in wax from which they are only released during
the wash.

Another wide spread use of enzymes is that of pectinases in food modification.

Pectin is a substance which, is found in cell walls and helps to hold the structure
together. Pectinase is the name given to a group of enzymes which, break down
pectins. They are therefore used to partially digest fruit and vegetables in baby food and to help extract
fruit/vegetable juices.
Water

Water is important because it is a major component of cells, typically forming between 70 and 95% of
their mass and it provides an environment for aquatic organisms. It's molecules have an imbalance of
charge (dipolar) and this generates hydrogen bonding between them.

Water as a solvent

Water is an excellent solvent for ions and polar molecules (molecules with an uneven charge) because
the water molecules are attracted to them, collect around them and separate them, so that they
dissolve. The chemicals are then free to move around and react with other chemicals and most
processes taking place in living organisms, happen like this in solution. Non-polar molecules like lipids do
not dissolve in water and tend to be pushed together by it. This is important in hydrophobic interactions
in protein structure and in membrane structure. Due to its ability to dissolve so many molecules, water is
an important transport medium in animals and plants.

Thermal properties

Water molecules are attracted to one another by hydrogen bonds and this restricts the movement of the
molecules. This means that a relatively large amount of energy is required to increase the temperature
of water (it has a high specific heat capacity) and that large bodies of water are slow to change
temperature e.g. lakes and oceans. Due to their high water content, the bodies of organisms are also
slow to change temperature and this makes maintaining a stable body temperature easier.

Water also requires a relatively high amount of energy to become a gas and this can be used as an
effective means of cooling the body by sweating and panting. Conversely, a relatively large amount of
energy must be transferred away from water to make it freeze, which is important for organisms with a
high body water content and for those living in water.

Density and freezing properties

Water is unusual because it's solid form is less dense than it's liquid form. Below 4°c the density of water
starts to decrease and so ice floats on water and insulates the water below it. This reduces the chances
of large bodies of water completely freezing and increases the chances of life in water surviving. These
changes in density of water with temperature are important in the oceans because they set up currents,
which circulate nutrients.

High surface tension and cohesion

Water molecules tend to stick together and this is exploited in the way that
water moves in long unbroken columns through the xylem tissue of plants and
is an important property in cells. The cohesion of water molecules generates a
surface tension at the surface of water enabling small organisms e.g. pond
skaters to exploit it as a habitat.

Inorganic ions

All of the other substances described in this topic are made up of molecules or groups of atoms but
individual atoms in the form of ions are also important to living organisms. Ions are formed when atoms
gain or loose electrons and are therefore positively or negatively charged.

Table showing the role of some important ions in living organisms

Ion Role in living organism

Calcium phosphate is an important structural component of bones and teeth. Calcium

Calcium Ca2+ ions are important in the transmission of nervous impulses and in the contraction of
muscles.

Involved in the transmission of nervous impulses and used in the kidney to reabsorb
Sodium Na+
water and produce concentrated urine.

Also involved in nervous transmission and contributes to turgidity in guard cells which
Potassium K+
control stomatal opening.

Magnesium Chlorophyll molecules contain magnesium. Some enzymes which catalyse the breakdown
Mg2+ of ATP have these ions at their active sites.

Also used in the kidney to produce concentrated urine. Chloride ions help to balance the
Chloride Cl-
positive charge of sodium and potassium ions in cells.

Nitrate NO3- Plants use the nitrogen in these ions to make proteins.

Phosphate Used for making nucleotides and with calcium, make calcium phosphate that gives bones
PO43- their strength.
This technique separates out mixtures of chemicals by using their different solubilities in certain
solvents. A concentrated spot of the solution to be separated is placed at one corner of a strip of paper.
This is dipped in a solvent which carries the dissolved chemicals up the paper depositing them, the least
soluble first, the most soluble last... If necessary, other chemicals may be used to make the spots visible
e.g. Ninhydrin colours amino acids. They are identified by their colour and Rf values:

Spots may be further separated by running a different solvent at right angles to the first (two-way
chromatography).