PROTEINS

WHAT IS
- Proteins are molecules
PROTEINS? composed of chain of amino
acid.

FUNCTIONS OF PROTEINS

 Enzymes
 Antibodies
 Actin and Myosin
 Collagen
 Keratin
 Antigens
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 acid.

 Amino acid 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 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.
 AMINO ACIDS

HYDROPHILIC HYDROPHOBIC

NOTE: You need to know this table

 STRUCTURE OF AMINO ACID

Each amino acid contains a central C atom, an amino

group(NH2), a carboxyl group(COOH), and a specific R group.

AMINO GROUP: consists of a nitrogen(N) atom attached by

single bonds to hydrogen(H) atoms, alkyl groups, aryl groups, or
combination of these three.

R- GROUP: Is a side chain specific to each amino acid that

confers particular chemical properties to that amino acid.

CARBOXYL GROUP: consists of carbon double- bonded to an oxygen(O) and

also bonded to a –OH group. An organic compound that contains a carboxyl
group[C[=O]OH]is carboxylic acids or organic acids.
EXPLANATION…

Each amino acid is attached to another amino acid by a

covalent bond, known as peptide bond.

Peptide Bond form between the Carboxyl group of one

amino acid and the amino group of another through
dehydration synthesis.

The reaction removes a Oxygen[O] atom from one

amino acid and 2 Hydrogen[H] atom from the amino
group of another amino acid.
A water molecule[O-HH] or H2O is released during the
process.
PROTEINS CAN BE DIVIDED INTO TWO
GROUPS

 Globular protein. These are molecules that are often

spherical in shape and have a chemical function e.g.
Enzymes.

 Fibrous protein. These have a structural role. They

give strength or elasticity to a particular tissue, e.g.
Keratin in hair.
 CHARACTERISTICS OF GLOBULAR
PROTEINS
 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.

 STRUCTURE AND FUNCTION OF GLOBULAR
PROTEINS

 The shape of a globular protein is very delicate and

vital to it’s function.

 An enzymes 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.
DIFFERENCES OF FIBROUS AND GLOBULAR
PROTEINS
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 form 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 protein, their shape is
vital to their function. E.g.. Enzymes.

Quaternary structure. The protein consists of more than one

polypeptide. The different polypeptide chains bind together to
form a whole molecule. E.g. insulin is made up of two
polypeptide chains whilst haemoglobin is made up of four.
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.