🧬 Protein Structure and Functions – Medium Note
🔹 Protein Structure
Proteins are large biomolecules made up of amino acids
linked by peptide bonds. The structure of a protein is essen-
tial to its function and is organized into four levels:
🧬 Amino Acids and Proteins
1. What are Amino Acids?
· Amino acids are the building blocks of proteins.
· Each amino acid contains:
o Amino group (-NH₂)
o Carboxyl group (-COOH)
o A unique side chain (R group)
There are 20 standard amino acids, which take part in the
formation of proteins. These are categorised into two groups as
following:
1. Essential Amino Acids (must be taken from food)
· Histidine
· Isoleucine
· Leucine
· Lysine
· Methionine
· Phenylalanine
· Threonine
· Tryptophan
· Valine
(b) Non-Essential Amino Acids (synthesized by the body)
· Alanine
· Arginine
· Asparagine
· Aspartic acid
· Cysteine
· Glutamic acid
· Glutamine
· Glycine
· Proline
· Serine
· Tyrosine
Classification of Proteins
1 ۔Based on the molecular shape, proteins can be classified into
two types.
1. Fibrous Proteins:
When the polypeptide chains run parallel and are held together by
hydrogen and disulfide bonds, then the fiber-like structure is
formed. Such proteins are generally insoluble in water. These are
water-insoluble proteins.
Example – keratin (present in hair, wool, and silk) and myosin
(present in muscles), etc.
2. Globular Proteins:
This structure results when the chains of polypeptides coil around
to give a spherical shape. These are usually soluble in water.
Example – Insulin and albumins are common examples of
globular proteins.
2. Types of Proteins (Based on Function)
1. Primary Structure
Linear sequence of amino acids in a polypeptide chain held to-
gether by strong peptide (covalent) bonds. Determines the overall
structure and function of the protein.
Example:
1. Insulin
Chain A (21 amino acids)
Chain B (30 amino acids)
2. Oxytocin (a peptide hormone, 9 amino acids):
Cys–Tyr–Ile–Gln–Asn–Cys–Pro–Leu–Gly
Secondary Structure
The secondary structure of a protein refers to the local folding
or coiling of the polypeptide chain into specific patterns, primarily
due to hydrogen bonding between the backbone atoms (not the
side chains) of amino acids ۔It Involves hydrogen bonds between
the carbonyl group (-C=O) of one amino acid, and the amide
group (-NH) of another amino acid. The folding creates regular,
repeating patterns that help stabilize the protein.
Types of Secondary Structure:
1. Alpha Helix (α-helix):
A right-handed spiral structure. Each turn of the helix
contains about 3.6 amino acids. Hydrogen bonds form
between every 4th amino acid. Found in keratin (hair, nails)
and myoglobin.
2. Beta Pleated Sheet (β-sheet): Polypeptide chains lie side
by side, forming a sheet-like structure. Can be parallel
(same direction) or antiparallel (opposite directions). Held
together by inter-chain hydrogen bonds. Found in silk
fibroin.
2. Tertiary Structure:
3D structure formed by further folding of the chain. Stabilized
by hydrogen bonds, disulfide bridges, ionic bonds, and van
der Waals forces. Determines the biological activity of the
protein.
1. Myoglobin
A globular protein that stores oxygen in muscle cells.
Mostly made of α-helices folded into a compact ball-like shape with
a heme group at the center.
2. Lysozyme
An enzyme in tears and saliva that breaks down bacterial cell
walls.
Has both α-helices and β-sheets folded into a stable, compact
globular form.
3. Ribonuclease A
A pancreatic enzyme that cuts RNA.
Its tertiary structure is stabilized by four disulfide bonds.
4. Immunoglobulin G (IgG) – Fab fragment
An antibody with β-sheet-rich domains folded into a specific Y-
shaped structure.
5. Insulin (after folding)
Two separate polypeptide chains (A and B) linked by disulfide
bridges, giving it its functional 3D shape.
3. Quaternary Structure:
Formed when two or more polypeptide chains (subunits)
combine. Example: Hemoglobin has four subunits.
Examples
1. Hemoglobin
Composed of 4 subunits: 2 α-chains + 2 β-chains.
Each subunit has its own heme group for oxygen binding.
2. DNA polymerase
Multiple subunits work together for DNA replication.
3. Collagen
A fibrous protein with 3 polypeptide chains wound into a triple
helix.
4. ATP synthase
A large enzyme complex with many subunits that makes ATP in
mitochondria.
5. Immunoglobulin G (IgG)
Y-shaped molecule made of 2 heavy chains + 2 light chains, linked
by disulfide bonds.
Functions of Proteins
Proteins play a wide variety of roles in living organisms:
(1) Structural Support – Provide strength and support (e.g.,
collagen, keratin).
(2) Enzymatic Activity – Act as enzymes to speed up chemi-
cal reactions (e.g., amylase, pepsin).
(3) Transport – Help transport substances (e.g., hemoglobin
transports oxygen).
(4) Defense – Involved in immunity (e.g., antibodies fight in-
fections).
(5) Hormonal Regulation – Some hormones are proteins
(e.g., insulin controls blood sugar).
(6) Movement – Responsible for muscle contraction (e.g.,
actin, myosin).
(7) Storage – Store essential substances (e.g., ferritin stores
iron).