Structure of Proteins

Proteins: Structure and function
 Proteins represent the structural composition of all living organisms. Proteins are
complex macromolecules (polymers). They have high molecular weight and are made up
of structural units (monomers) called amino acids.
Function of proteins
Proteins play a very important role in the body. They are involved in almost all the body
mechanisms. Some of their roles:
1. They're the main components of the Extracellular matrix (ECM) which have many
important functions such as, providing the mechanical and architectural support of the
cells and regulating cell activities such as migration, differentiation, proliferation
and Paracrine signaling.
2. Enzymes are proteins that accelerate, or catalyze, chemical reactions.
3. Transport: they bind and deliver specific molecules to organs or across cell membrane.
4. Motile: they provide mechanism for cell motion.
5. Defense: proteins integral to the immune response and coagulation mechanism.
6. Regulatory: like Cytokines which regulate cell activity.
7. Some hormones like insulin are proteins
Structure of proteins
Proteins have four different levels of structure – primary, secondary, tertiary and quaternary.
1. Primary Structure
 The linear sequence of amino acids joined together by peptide bond is termed as the
primary structure of the protein.
 When the amino group of an amino acid combines with the carboxyl group of another
amino acid, a peptide bond is formed.
 The higher level of organization in proteins depends on the primary structure of proteins.
 A change in single amino acid can cause a disease like sickle cell anemia.
2. Secondary Structure
 This describes the way by which polypeptides are coiled. This structure is formed as a
result of the hydrogen bonds between carboxyl and amine groups in close amino acid
monomers.
 The two main types of secondary structure are the α-helix and the ß-sheet:
1. α-helix: The backbone follows a helical structure. The hydrogen bonds with the oxygen
between the different layers of the helix, giving it this helical structure. Presence of amino
acids such as alanine, leucine, and glutamine help to form strong helical structures while
presence of proline disrupts the helical structure. α-helix are found in many proteins like
myoglobin.
2. β-pleated sheet: here the polypeptide chains are stacked next to each other and their outer
hydrogen molecules form intramolecular bonds to give it this sheet-like structure. The β-
pleated sheet can be parallel (sheets run in same direction) or antiparallel (strands in sheet
run in opposite direction)
3. Tertiary Structure:
The final 3D structure of a protein, entailing the shaping of a secondary structure. The protein
molecule bend and twist in such a way so to achieve maximum stability or the lowest energy
state.
Tertiary structure is held together by four different bonds and interactions:
 Disulphide Bonds - Where two Cysteine amino acids are found together, a

strong double bond (S=S) is formed between the Sulphur atoms within the
Cysteine monomers.
 Ionic Bonds - If two oppositely charged ‘R’ groups (+ve and -ve) are found close
to each other, and ionic bond forms between them.
 Hydrogen Bonds
 Hydrophobic and Hydrophilic Interactions - Some amino acids may be
hydrophobic while others are hydrophilic. In a water based environment, a
globular protein will orientate itself such that its hydrophobic parts are towards its
centre and its hydrophilic parts are towards its edges.
 Van der waal’s forces.
4. Quaternary Structure
 This describes proteins which consist of two or more chains of polypeptides. This
structure is formed as a result of the linkage of polypeptide chains with each other.
 Many proteins are made up of multiple polypeptide chains, often referred to as protein
subunits.
 The quaternary structure refers to how these protein subunits interact with each other and
arrange themselves to form a larger aggregate protein complex.
 The final shape of the protein complex is once again stabilized by various interactions,
including hydrogen bonding, disulfide-bridges and salt bridges

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Proteins: Structure and function

Tertiary structure is held together by four different bonds and interactions:

 Disulphide Bonds - Where two Cysteine amino acids are found together, a

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