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
• Oxygen transport
• Keratin
• Hormones
• Membrane formation
 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.
2- Secondary structure:
Results from hydrogen bond
formation between hydrogen of –NH
group of peptide bond and the carbonyl
oxygen of another peptide bond.
According to H-bonding there are two
main forms of secondary structure:
α-helix: It is a spiral structure resulting
from hydrogen bonding between one
peptide bond and the fourth one
β-sheets: is another form of secondary
structure in which two or more
polypeptides (or segments of the same
peptide chain) are linked together by
hydrogen bond between H- of NH- of one
chain and carbonyl oxygen of adjacent
chain (or segment).
• 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.
• Tertiary structure
is determined by a variety of
interactions (bond formation) among R
groups and between R groups and the
polypeptide backbone.
a. The weak interactions include:
 Hydrogen bonds among polar side
chains
 Ionic bonds between
charged R groups ( basic and acidic
amino acids)
 Hydrophobic
interactions among
hydrophobic ( non polar) R
groups.
b. Strong covalent bonds include disulfide bridges,
that form between the sulfhydryl groups (SH) of
cysteine monomers, stabilize the structure.
• Quaternary structure: results from the aggregation (combination) of two or more
polypeptide subunits held together by non-covalent interaction like H-bonds,
ionic or hydrophobic interactions.
• Examples on protein having quaternary structure:
– Collagen is a fibrous protein of three polypeptides that are supercoiled like
a rope.
• This provides the structural strength for their role in connective tissue.
– Hemoglobin is a globular protein with four polypeptide chains
– Insulin : two polypeptide chains
 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.
• 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 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.