Proteins.

Function of proteins.

 Proteins are very important in living organisms

and take on a variety of forms and functions:
 Enzymes.
 Antibodies.
 Actin and myosin
 Collagen.
 Keratin
 antigens
 The structure of proteins.
 Proteins are made up of carbon,
hydrogen, oxygen and nitrogen.
Sometimes sulphur is present.
 Proteins are polymers made up of the
monomers called amino acids.
 There are 20 different amino acids.
 Amino acids can join up in any order and
form an infinite number of protein
molecules.
 Amino acids.
 Amino acids contain an amino group
(-NH²) and a carboxylic acid group
(-COOH).
 Each amino acid has an R group.
 There are 20 different R groups and this is
the reason for there being 20 different
types of amino acids.
 Structure of an amino acid.
R
Group

Amino Carboxylic acid

group group
 How do two amino acids join
together ?
 Two amino acids join together by
condensation to form a dipeptide .

A peptide
bond is
formed and
this results in
a dipeptide
 What is a polypeptide?
 A chain of amino acids is known as a
polypeptide.
Proteins can be divided into groups.
 Globular proteins. These are molecules
that are often spherical in shape and have
a chemical function eg enzymes.
 Fibrous proteins . These have a structural
role . They give strength or elasticity to a
particular tissue eg keratin in hair.
 Four levels of structure.
 Primary structure. A sequence of amino
acids in a polypeptide chain.
 Secondary structure. The chain of amino
acids bend and twist and forms a stable
structure that is held in position by
hydrogen bonds. A helix is the most
common secondary structure.
 Tertiary structure. The secondary structure
folds to give a more three dimensional
shape. The shape is maintain by hydrogen
bonds and the stronger disulphide bridges
which form between the sulphur containing
amino acids molecules.
 Such proteins are often called globular
proteins. their shape is vital to their
function. Eg enzymes.
 Quaternary structure- the protein
consists of more than one polypeptide.
The different polypeptide chains bind
together to form a whole molecule. Eg
insulin is made up of two polypeptide
chains whilst haemoglobin is made up
of four.
 Haem
group

Haemoglobin is
made up of 4
different
polypeptide
chains.

Haemoglobin molecule
Keratin is a secondary
structure protein. it has
a spiral shape and is
held in position by
hydrogen bonds.
 Globular proteins.
 Globular proteins have the following
characteristics:
 Irregular amino acid sequence
 Sequence is highly specific and never varies
between 2 examples of the same protein.
 Polypeptides fold into a spherical shape.
 Relatively unstable structure.
 Metabolic functions.
 Egs enzymes, hormones and haemoglobin.
Enzymes.
 Structure and function of globular
proteins.
 The shape of a globular protein is very delicate
and vital to it’s function.
 An enzyme has a precise tertiary structure that
provides it with it’s active site. Any change in the
shape of the active site will stop the enzyme
from working.
 High temperatures make the molecules vibrate
and this causes the weak hydrogen bonds to
break and as a result the shape changes. The
enzyme is denatured and will not work.
 Denaturation of proteins.
 The three dimensional shape of proteins is
maintained by hydrogen bonds and ionic
bonds which are fairly weak.
 Any agent such as heat, acids or alkalis
will break these bonds and cause a
change in shape.
 With a change in shape the protein can no
longer carry out it’s function.
 Questions.
1 Describe the general structure of an amino
acid.
2 With the aid of a diagram , show the
results when two amino acids are joined
together.
3 Proteins may be described as having:
4 Primary, secondary, tertiary or quaternary
structures. Explain the meanings of these
terms when applied to proteins.
5 Describe the characteristics of a globular
protein.
6 How is the structure of a globular protein
related to it’s function?

7 What is meant by the term denatured?

8 Explain how a protein may become
denatured.