2.

5
Proteins
Specification
reference: 3.1.2
 Learning Objectives
• How are amino acids linked to form
polypeptides – the primary structure of proteins?
• How are polypeptides arranged to form the
secondary structure and then the tertiary
structure of a protein?
• How is the quaternary structure of a protein
formed?
• How are proteins identified?
 Starter Activity: Word-Search
ALPHA HELIX
AMINO ACID
D Y P O L Y P E P T I D E D H
BIURET
N R D I C A O N I M A F I H A CONDENSATION
O A N X Z Z L H S C E S Y K E DIPEPTIDE
B N O T I Q Y T U W U D P D M DISULPHIDE BOND
N R B E Y L M I E L R C N P O GLOBULAR
E E C R E Q E Y P O B O G R G HAEMOGLOBIN
G T I U Q D R H L V B F L O L HYDROGEN BOND
O A N I I A I Y A E K R O S O HYDROLYSIS
R U O B I D S T D H E I B T B IONIC BOND
D Q I T E I A I P M P S U H I MONOMER
Y C R B S J T O Y E S L L E N PEPTIDE BOND
H E O C R P I L C E P S A T C POLYMER
POLYMERISATION
T N H R E M O N O M R I R I N
POLYPEPTIDE
D A R P W P N V O B F R D C Q
PROSTHETIC
N O I T A S N E D N O C E W W TERTIARY
QUATERNARY
Why are Proteins
polymers?
Proteins consist
of long chains of
amino acids.
 There are over 20 naturally
occurring amino acids, which
differ in the composition of
the R group.
Two amino acids may be
linked together by a
condensation reaction to
form a ‘dipeptide’.
Since the amino acids may be joined in any
sequence there is an almost infinite variety of
possible proteins.
•The chain of amino acids is referred to as the
protein’s primary structure.
•The chain is folded (often into a helix) to give
the secondary structure.
•The secondary structure is folded on itself to
form the tertiary structure.
•The combination of a number
of polypeptide chains along with
associated non-protein groups
results in the quaternary.
Quaternary Structure Of A
Protein
•These shapes are due to the fact
that proteins are amphoteric, i.e.
they have both positive and
negative charges on them.
•The attraction of these opposite
charges forms weak electrostatic
(hydrogen) bonds causing the
chain to form a complex 3D
structure – globular proteins.
•Ionic bonds, disulphide bridges,
hydrogen bonds and hydrophobic
interactions all contribute to the
final shape of a given protein
molecule.
 All enzymes and some
hormones are globular
proteins and their functions
depend on the precise shape
of the protein molecule.
•Sometimes the protein consists of
long parallel chains with cross-links –
fibrous proteins.
•These are insoluble and have
structural functions, e.g. collagen in
cartilage; keratin in hooves, feathers
and hair, actin and myosin in muscle.
 If a globular protein is heated
or treated with a strong acid or
alkali the hydrogen bonds are
broken and it reverts to a more
fibrous nature – a process
called DENATURATION.
 Proteins sometimes occur in
combination with a non-
protein substance (prosthetic
group); these are called
conjugated proteins, e.g.
haemoglobin.
 Test for Proteins
The Biuret test detects peptide bonds.
• Place a sample of the solution to be tested in a test tube and add an
equal volume of sodium hydroxide solution at room temperature.
• Add a few drops of very dilute (0.5%) copper (II) sulphate solution
and mix gently.
• A purple coloration indicates the presence of peptide bonds and
hence a protein. If no protein is present, the solution remains blue.
• Alternatively use Biuret reagent to test for protein. A purple colour
shows protein is present; a blue colour indicates that protein is
absent.
 Protein shape and function
Proteins perform many different roles in
living organisms. Their roles depend on
their molecular shape, which can be of 2
basic types.
• Fibrous proteins, such as collagen, have
structural functions.
• Globular proteins, such as enzymes and
haemoglobin, carry out metabolic functions.
It is the very different structure and shape
of each of these types of proteins that
enables them to carry out their functions.
Fibrous Proteins e.g. Collagen
These form long chains which run parallel to one
another. These chains are linked by cross-bridges
and so form very stable molecules. One example
is collagen. Its molecular structure is as follows:
• The primary structure is an unbranched
polypeptide chain.
• In the secondary structure the polypeptide chain
is very tightly wound.
• In the tertiary structure the chain is twisted into a
second helix.
• Its quaternary structure is made up of 3 such
polypeptide chains wound together in the same
way as individual fibres are wound together in a
rope.
Collagen is found in tendons.
Tendons join muscles to bones.
When a muscle contracts the bone is
pulled in the direction of the
contraction. The individual collagen
polypeptide chains in the fibres are
held together by cross-linkages
between amino acids of adjacent
chains.

•The points where one collagen

molecule ends and the next begins
are spread throughout the fibre
rather than all being in the same
position along it.
 Questions
1. Explain why the quaternary structure of
collagen makes it a suitable molecule for a
tendon.
2. Suggest how the cross-linkages between the
amino acids of polypeptide chains increase the
strength and stability of a collagen fibre.
3. Explain why the arrangement of collagen
molecules is necessary for the efficient
functioning of a tendon.
 Answers
1. It has 3 polypeptide chains wound together to form a
strong, rope-like structure that has strength in the
direction of pull of a tendon.
2. It prevents the individual polypeptide chains from
sliding past one another and so they gain strength
because they act as a single unit.
3. The junctions between adjacent collagen are points
of weakness. If they all occurred at the same point in
a fibre, this would be a major weak point at which
the fibre might break.
Plenary: Use the following key words to write
an essay on proteins. You must include all key
words! Monomer
Amino Acid Peptide Bond
Biuret Polymer
Condensation Polymerisation
Dipeptide Polypeptide
Disulphide Bond Primary
Globular Prosthetic
Haemoglobin Secondary
Hydrogen Bond Tertiary
Hydrolysis Quaternary
Ionic Bond Alpha Helix
 Learning Objectives
• How are amino acids linked to form
polypeptides – the primary structure of proteins?
• How are polypeptides arranged to form the
secondary structure and then the tertiary
structure of a protein?
• How is the quaternary structure of a protein
formed?
• How are proteins identified?