Protiens

Describe the basic structure of an amino acid (structures of specific amino acids are not required) and
the formation of polypeptides and proteins (as amino acid monomers linked by peptide bonds in
condensation reactions) and explain the significance of a proteins primary structure in determining its
three-dimensional structure and properties (globular and fibrous proteins and types of bonds involved in
threedimensional structure).

Amino acids

Amino acids are the monomers involved in protein synthesis. Many amino acids joined together
by peptide bonds formed by condensation reactions form polypeptide chains.

the R group is the variant. There can be 20 different r groups for the 20 different amino acids.
For example, it could be CH3, CH2SH, CH2NH2

Formation of a peptide bond

a peptide bond forms between the two amino acids after the removal of water.
Many amino acids joined up in this way result in a polypeptide chain forming
The peptide bond forms between the carboxylic group of one amino acid and the amino group
of the other

Primary structure

This is the number and sequence of amino acids in the polypeptide chain. The only form of
bonding present are the peptide linkages
Proteins differ from one another by varying their number and sequence of a. acids. Each type of
protein has a unique primary structure.
There are more types of proteins than carbohydrates. Glycogen and starch have only one type
of monomer whereas proteins can have various kinds of amino acids
Tertiary structure

This is the final folding of the polypeptide chain into a compact, globular shape
This 3D structure is maintained by ionic bonds, hydrogen bonds and disulphide bridges formed
between R groups
Fibrous proteins lack a tertiary structure as they show limited folding and therefore lack a
specific shape.
The folding will take place so that nonpolar groups are on the inside and the polar group face
outwards.

How does the primary structure determine tertiary structure:

The primary structure is the sequence of amino acids in the polypeptide chains. amino acids are
joined by peptide bonds
The primary structure determines the sequence of R groups. The polypeptide chain folds in such
a way so that ionic, hydrogen and disulphide bonds can form between R groups. These bonds
maintain the tertiary structure.
Different proteins have different primary structures so each polypeptide chain will fold in a
different way giving a different tertiary structure.
The tertiary structure is the final folding of the polypeptide chain to form a compact globular
shape and this is maintained by the ionic, hydrogen and disulphide bonds between R groups
The polypeptide chain folds so that the polar R groups point outwards and the non-polar R
groups point inwards

How are amino acids 57 and 58 joined: since they are adjacent they are joined by peptide bonds to
form a dipeptide

How are amino acids 22 and 141 brought close together: the polypeptide chain folds in such a way so
that amino acids 22 and 141 are in a suitable position for their r groups to forms a suitable bond

In enzymes, the tertiary structure determines the shape of the active site making the enzyme
highly specific
The tertiary structure is responsible for the specificity of some proteins enzymes and
hormones
Enzymes are globular meaning they are soluble in water and as they have many polar R groups

Function of R groups in proteins;

I,h,d bonds formed between the R group maintain the tertiary structure.
R groups affect the solubility of the protein.
The nature and interaction of R groups determine the final folding of the polypeptide chain,
which in turn determines its specific shape

Globular and Fibrous protein:

Proteins can be either of the two

Fibrous proteins lack a tertiary structure as their polypeptide chain shows limited folding. They
then lack a specific shape and specificity.
 Fibrous proteins are usually linear. Globular are more compact due to folding in the ppeptide
chain
Glob is soluble, fibr is insoluble
Fibrous are long and contain many amino acids which are in a repetitive sequence. Glob are not
repetitive. In fib the polypeptide chains lay next to each other and there are bonds linking the
chains together.
Fibrous has more amino acids than globular
Enzymes, antibodies, fibrinogen and hemoglobin are globular as they have a specific shape and
their functions depend on their shape
Fibrous proteins are structural such as keratin, fibrin and collagen

At high temps or extremes of Ph, the 3D structure of the protein is disrupted. Bonds holding it together
are destroyed and the protein is said to be denatured. When heated over 50 degrees the length of the
polypeptide chain increases as the bonds maintaining structure break due to increased atomic
vibrations. The polypeptide chain unravels. In the case of enzyme, the active site is altered.
bonds holding the tertiary structure break (and the tertiary structure determine the shape of the
active site), therefore the polypeptide unravels and the shape if the active site is altered and the
substrate of complementary shape can no longer bind.

Role of ionic bonds: between two oppositely charged R groups