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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.

- The primary structure depends on the order and number of amino acids in a particular
protein.

- There are enormous range of possible structures

- For example: Haemoglobin is made up of 4 polypeptide chains, 2 chains and 2 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
- Polypeptide chain may coil into an -helix due to the attraction between the oxygen of the
CO group of one amino acid and the hydrogen of the NH group of another amino acid to
form hydrogen bond.

- Some produce a looser -pleated sheet (again held together by hydrogen bonds)

- Hydrogen bonds are strong enough to hold the 2
o
structure but are easily broken by high
temperature or changes in pH








Tertiary structure of proteins
- The polypeptide helix shape twists and folds itself to produce a 3D shape

- The shape is very precise with amino acids held in an exact shape by:
Hydrogen bonds
Disulfide bonds
Ionic bonds
Hydrophobic interactions


Quaternary structure of proteins
- If a protein is made up of several polypeptide chains, the way they are arranged is called
the quaternary structure.

- The chains are held together by the same types of bond seen in tertiary structure

- Again, each protein formed has a precise and specific shape (e.g. haemoglobin)

Globular proteins
Proteins structures are divided into two groups:
Fibrous proteins
Globular proteins:
o Compact molecules where the highly twisted polypeptide chains rolls up into a ball.
o The amino acids with the hydrophobic groups point to the centre of the molecule and so
water is excluded from the centre of the folded protein molecule.
o The amino acids with the hydrophilic groups are on the outside and so globular proteins are
usually soluble.

Fibrous proteins:
o Consists of polypeptides laid down in parallel chains forming long fibres or sheets
o They are usually insoluble.


Comparison of globular and fibrous proteins

Globular Fibrous
Relatively unstable structure Very stable
Soluble Insoluble
Polypeptide chains rolls up into spherical
structure
Polypeptide chains form long strands in parallel
chains forming long sheets
E.g. Haemoglobin, Hormone(insulin) E.g. Collagen (Found in bones, cartilage,
wall of arteries)


Difference between Haemoglobin and Collagen
Haemoglobin Collagen
It is a globular protein It is fibrous protein
Consists of 4 polypepteide chains; 2 identical
-helix & 2 deifferent -pleated
Consists of 3 polypeptide chains wound around
to form triple helix (like a rope with three
strands)
Molecule is nearly spherical (held together with
the forth chain held close together by
disulphide bond)
Almost every third of amino acids is glycine.
Its small size allows it to lie together in atight
coil.
Each iron ion (Fe
2+
) can combine with an
oxygen molecule so a complex molecule of 4
haem groups can combine with an oxygen
molecule.
Each 3 complete stranded molecules interact
with other 3 stranded molecules running
parallel to it

At the centre of each chain, is an ion (Fe
2+
)
containing group called haem.
The end of the parallel strands (helices) are
staggered and this adds to the great tensile
strength making collagen very difficult to
break.
Picks up oxygen in the lungs to become
oxyhaemoglobin which readily dissociate
(easily breaks down) in the tissue to release its
oxygen and revert back to haemoglobin.
The cross links hold many collagen molecules
to form fibres
Bonds from between the R groups in lycines
molecules lying next to each other
The strands are held together by hydrogen
bond

Summary:
Proteins structure No. of polypeptide chains structure
1
o
1 Long chain
2
o
1 H bonds from -helix or -sheets
3
o
1 2
o
structure folded into 3D shape
held by 4 types of bond 4
o
More than 1

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.

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