Secondary structure

This level of protein structure refers to the localised folding of the polypeptide
chain into repeating units. Of the different possible secondary structures the
most widely observed are the Alpha-helix ( helix) and the Beta- sheet ( sheet).
These structures are stabilised by numerous intermolecular interactions called
hydrogen bonds (electrostatic attraction which exists between polar molecules
consisting of a hydrogen atom bound to electronegative atoms such as N, O or
F).
helix

In alpha helix structure, hydrogen bonding exists between the carbonyl

oxygen (CO) of one amino acid residue (part of amino acid which remains
after peptide bond formation) and the amide proton (NH) of another
residue separated by 4 residues in the direction of the C-terminus.
The hydrogen bonds exist between the residues of a single polypeptide
chain and are almost parallel to the axis of this chain.

sheet

In the beta sheet structure, hydrogen bonding exists between the carbonyl
oxygen of a residue on one chain and the amide proton of a residue on an
adjacent chain.
These hydrogen bonds are almost perpendicular to the axis of the chains.

Tertiary structure
This refers to the overall 3 dimensional folding of the monomeric protein (no
quaternary structure) or the protein subunit (has a quaternary structure). This
particular structure is stabilised by a range of interactions including:
-

Hydrogen bonds
Ionic bonds (salt bridges)
Hydrophobic interactions
Disulphide bonds (S-S)

The tertiary structure involves packing away hydrophobic (water hating) side
chains at the protein centre where they wont encounter water and placing of
hydrophilic (water loving) side chains at the surface where they will encounter
water.

Why is protein folding so important

Proteins are an essential building block of life, making up numerous structures
such as hair (keratin), tissue (e.g. collagen). In addition, proteins also form
enzymes (biological catalysts which enhance chemical reactions without being
used up) which ensure that metabolic processes within the body are optimal.
Consequently it is apparent that proteins have a range of biological functions. It
is the very folding of the protein itself which makes it unique and determines its
particular role in biological systems. All four levels of protein structure (primary,
secondary, tertiary and quaternary determines function) contribute to the final
shape of the protein.
In enzymes, the folding of the protein determines the shape of the active sitethe region of the enzyme where a particular substrate (a molecule) binds to. This
controls the particular reaction the enzyme is able to catalyse.