Protein Structure
Protein structure is defined as a polymer of amino acids joined by peptide bonds. There
are 4 levels of protein structure – primary, secondary, tertiary and quaternary.
1. Primary Structure of Protein ( 1o ):
The primary structure of a protein refers to the order of amino acid residues in
the polypeptide chain of the protein.
This is the exact ordering of amino acids i.e., just a list of which amino acids
appear in which order in a polypeptide chain
chain.
The free α-amino group, written to the left, is called the amino-terminal
amino or N-
terminal end.
The free α-carboxyl group, written to the right, is called the carboxyl-terminal
carboxyl or
C-terminal end.
The amino acid sequence is unique to the protein and is the basis for
understanding its structure and function.
Covalent, peptide bonds which connect the amino acids together maintain the
primary structure of a protein.
Secondary Structure of Protein ( 2o ):
Secondary structure of protein refers to local folded structures that form within a
polypeptide due to interactions between atoms of the backbone.
This structure arises due to the regular folding of the backbone of the polypeptide
chain due to hydrogen bonding between -CO group and -NH NH groups of different
amino acid residues of the peptid
peptide bond.
Hydrogen bonds stabilize Secondary structure of protein.
They are found to exist in two different types of structures α – helix and β – pleated
sheet structures.
α-helix:
helix: The backbone follows a helical structure.
β – pleated sheet : the hydrogen bonds occur between residues on neighbo neighbouring
peptide chains forming sheet
sheet-like structure.
Tertiary Structure of Protein ( 3o or 3D ):
The tertiary structure of a polypeptide chain is its overall three
three-dimensional
dimensional shape
This structure arises from further folding of the secondary structure of the protein.
Multiple noncovalent interaction slike H-bonds,
bonds, electrostatic forces, disulphide
linkages, and Vander Waals forces stabilize this structure.
It gives rise to two major molecular shapes called fibrous and globular.
Quaternary Structure of Protein ( 4o ):
The spatial structure formed by the interaction of two or more polypeptide chains
is called the quaternary structure.
Quaternary structure only applies to multi-subunit proteins; that is, proteins made
from more than one polypeptide chain. Proteins made from a single polypeptide will
not have a quaternary structure.
An example of this structure of a protein is hemoglobin (Hb). Each Hb molecule has 4
peptide chains, 2 α-chains and 2 β-chains forming a tetramer. All 4 subunits are linked
together via hydrogen bonds and hydrophobic interactions and no covalent bonds occur
between the sub-units.
2 α-chains
2 β-chains
( Structure of Haemoglobin )
Protein denaturation
The stability of protein and its structure depends on physical and chemical
[Link], chemicals and pH affect their stability to a great extent.
Denaturation of the proteins is a condition when the unique three-dimensional
structure of a protein is exposed to changes.
A wide variety of reagents and conditions, such as heat, organic compounds, pH
changes, and heavy metal ions can cause protein denaturation.
Due to changes in temperature, pH or other chemical activities, the hydrogen bonds
present in the proteins get disturbed. This results in the unfolding of globular
proteins and uncoiling of the helix structure.
The uncoiling of helix structure affects the chemistry of proteins and they lose their
biological activity. This phenomenon of losing their activity and uncoiling of helix
structure due to physical or chemical changes is called the denaturation of proteins.
During the denaturation of proteins, the secondary and tertiary structures get
destroyed and only the primary structure is retained.
Covalent bonds are broken and interaction between amino-acid chains gets
disrupted. This results in the loss of biological activity of the proteins.
Biological Functions of Proteins
Proteins are a class of macromolecules that serve various functions in the body. These
range from digestion, transportation and structural functions to defense, storage and
movement.
Enzymes
Certain proteins act as enzymes. Enzyme are proteinaceous catalysts which regulate the
rate of biochemical or metabolic reactions.
Structural Proteins
Proteins are body builders. Proteins are integral part as they form components of certain
structureslike membranes, muscles, bones, cartilages, cytoskeleton etc.
Hormonal Functions
Hormones are paramount for regulating body functions. Insulin is one such example,
which regulate blood sugar level.
Transportation
Proteins play a major role in transporting substances throughout the body. Examples of
such proteins include haemoglobin which transport O2 and CO2 in blood. Carrier proteins
of cell membrane help in active transport.
Defence and Protection
Proteins form a part of the immune system and protect the body from pathogens. Example
of such a protein is antibodies or immunoglobulins.
Storage Functions
Proteins also provide nourishment for development of embryo – such as albumin, or the
egg white.
Movement
Actin and myosin proteins help in muscle movement.