Quaternary Structure of Protein

Quaternary Structure of Proteins

 A great majority of proteins are composed of single
polypeptide chains.
 Some of the proteins, however, consist of two or more
polypeptide which may be identical or unrelated.
 Such proteins are termed as oligomers and possess
quaternary structure.
 The individual polypeptide chains are known as
monomers, protomers or subunits
Bonds in quaternary structure
 The monomeric subunits are held together by non-
covalent bonds namely hydrogen bonds, hydrophobic
interactions and ionic bonds.
 Importance of oligomeric proteins : These proteins
play a significant role in the regulation of metabolism
and cellular function.
 The quaternary protein structure involves the clustering of
several individual peptide or protein chains into a final
specific shape.
 A variety of bonding interactions including hydrogen
bonding interactions including
Hydrogen bonding, salt bridges,
and disulfide bonds hold the
various chains into a particular
geometry.
 Two kinds of quaternary structures; both are multi
subunit protein
Homodimer : association between identical
polypeptide chains
Heterodimer : interaction between subunits of very
different structures.
 The interaction within multi subunits are the same as
that found in tertiary and secondary structures
 Quaternary structure adds stability by decreasing the
surface/volume ratio of smaller subunits
 Simplifies the construction of large complexes – viral
capsids and proteosomes
Example
 Hemoglobin is a globular protein with 4 polypeptide
chains bonded together.
 It therefore has a quaternary structure.
 There are 4 heam groups each contain iron.
 Each heam group can carry one molecule of oxygen.
 The four polypeptide chain consists of two alpha and
two beta chains.
Thank you