Unit 2: Proteins:-

What is an Amino acid?

“Amino Acids are the organic compounds that combine to form proteins, hence they are referred to as the
building components of proteins. These biomolecules are involved in several biological and chemical
functions in the human body and are the necessary ingredients for the growth and development of human
beings. There are about 300 amino acids that occur in nature.”

Amino acids are organic compounds containing the basic amino groups (-NH2) and carboxyl groups (-COOH).
The ingredients present in proteins are amino acids. Both peptides and proteins are long chains of amino
acids. Altogether, there are twenty amino acids, which are involved in the construction of proteins.

List of 20 Amino acids with the chemical formula

Listed below are the names of twenty amino acids along with their chemical formula.

Alanine C3H7NO2 Leucine C6H13NO2

Aspartic Acid C4H7NO4 Lysine C6H14N2O2

Asparagine C4H8N2O3 Methionine C5H11NO2S

Arginine C6H14N4O2 Proline C5H9NO2

Cytosine C4H5N3O Phenylalanine C9H11NO2

Cysteine C3H7NO2S Serine C3H7NO3

Glycine C2H5NO2 Tyrosine C9H11NO3

Glutamine C5H10N2O3 Threonine C4H9NO3

Histidine C6H9N3O2 Tryptophan C11H12N2O2

Isoleucine C6H13NO2 Valine C5H11NO2

➢ General properties of Amino acids:-

• They have a very high melting and boiling point.

• Amino acids are white crystalline solid substances.

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• In taste, few Amino acids are sweet, tasteless, and bitter.

• Most of the amino acids are soluble in water and are insoluble in organic
solvents.

Essential and Non-essential Amino acids:-

➢ Out of 20 amino acids, our body can easily synthesize a few on its own, which are called non-
essential amino acids. These include alanine, asparagine, arginine, aspartic acid, glutamic
acid, cysteine, glutamine, proline, glycine, serine, and tyrosine.
➢ Apart from these, there are other nine amino acids, which are very much essential as they
cannot be synthesized by our body. They are called essential amino acids, and they include
isoleucine, histidine, lysine, leucine, phenylalanine, tryptophan, methionine, threonine, and
valine.

Structure of Amino acids

➢ The general structure of Amino acids is H2NCH RCOOH, and it can be written as:

COOH

H2N – – C – – H

➢ There are 20 naturally occurring amino acids and all have common structural features – an
amino group (-NH3+), a carboxylate (-COO-) group and a hydrogen-bonded to the same
carbon atom. They differ from each other in their side-chain called the R group. Each amino
acid has 4 different groups attached to α- carbon.

These 4 groups are:

• Amino group,

• COOH,

• Hydrogen atom,

• Sidechain (R).

➢ Structure of 20 Amino acids with their chemical formula

Here is the structure of twenty amino acids with their chemical formula.
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Sources of Amino acids

➢ Amino acids play an important role in performing several biological and chemical functions in
different parts of our body, including building and repairing the tissues, the formation and
function of enzymes, food digestion, the transportation of molecules, etc. Our body can
synthesize only certain amino acids and the rest of the amino acids which are called essential
amino acids should be supplied through protein-rich foods in our daily diet.

➢ Foods rich in amino acids include plant-based products like broccoli, beans, beetroots,
pumpkin, cabbage, nuts, dry fruits, chia seeds, oats, peas, carrots, cucumber, green leafy
vegetables, onions, soybeans, whole grain, peanuts legumes, lentils, etc. Fruits rich in amino
acids are apples, bananas, berries, figs, grapes, melons, oranges, papaya, pineapple, and
pomegranates. Other animal products include dairy products, eggs, seafood, chicken, meat,
pork etc.
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Functions of Amino acids

➢ Functions of Essential Amino acids:-

• Phenylalanine helps in maintaining a healthy nervous system and in

boosting memory power.

• Valine acts as an important component in promoting muscle growth.

• Threonine helps in promoting the functions of the immune system.

• Tryptophan is involved in the production of vitamin B3 and serotonin

hormones. This serotonin hormone plays a vital role in maintaining
our appetite, regulating sleep and boosting our moods.

• Isoleucine plays a vital role in the formation of haemoglobin,

stimulating the pancreas to synthesize insulin, and transporting
oxygen from the lungs to the various parts.

• Methionine is used in the treatment of kidney stones, maintaining

healthy skin and also used in controlling invade of pathogenic
bacteria.

• Leucine is involved in promoting protein synthesis and growth

hormones.

• Lysine is necessary for promoting the formation of antibodies,

hormones, and enzymes and in the development and fixation of
calcium in bones.

• Histidine is involved in many enzymatic processes and in the

synthesizing of both red blood cells (erythrocytes) and white blood
cells (leukocytes).

➢ Functions of Non-Essential Amino acids:-

• Alanine functions by removing toxins from our body and in the

production of glucose and other amino acids.

• Cysteine acts as an antioxidant and provides resistance to our body;

it is important for making collagen. It affects the texture and
elasticity of the skin

• Glutamine promotes a healthy brain function and is necessary for

the synthesis of nucleic acids – DNA and RNA.

• Glycine is helpful in maintaining the proper cell growth, and its

function, and it also plays a vital role in healing wounds. It acts as a
neurotransmitter.

• Glutamic acid acts as a neurotransmitter and is mainly involved in

the development and functioning of the human brain.
 Unit 2: Proteins:-

• Arginine helps in promoting the synthesis of proteins and hormones,

detoxification in the kidneys, healing wounds, and maintaining a
healthy immune system.

• Tyrosine plays a vital role in the production of the thyroid hormones

-T3 and T4, in synthesizing a class of neurotransmitters and melanin,
which are natural pigments found in our eyes, hair, and skin.

• Serine helps in promoting muscle growth and in the synthesis of

immune system proteins.

• Asparagine is mainly involved in the transportation of nitrogen into

our body cells, formations of purines and pyrimidine for the
synthesis of DNA, the development of the nervous system and
improving our body stamina.

• Aspartic acid plays a major role in metabolism and in promoting the

synthesis of other amino acids.

➢ Proline is mainly involved in the repairing of the tissues in the

formation of collagen, preventing the thickening and hardening of
the walls of the arteries (arteriosclerosis) and in the regeneration of
new skin.

➢ Deficiency of Amino acids:-

As mentioned above, amino acids are the building blocks of proteins and proteins play a fundamental
role in almost all life processes. Therefore, it is necessary to include all nine essential amino acids in
our daily diet to maintain a healthy and proper function of our body. The deficiency of amino acids
may include different pathological disorders, including:

• Edema.

• Anemia.

• Insomnia.

• Diarrhea.

• Depression.

• Hypoglycemia.

• Loss of Appetite.

• Fat deposit in the liver.

• Skin and hair related problems.

• Headache, weakness, irritability, and fatigue.

✓ α-amino acids are the fundamental building blocks of proteins, characterized by an amino
group and a carboxyl group both attached to the same carbon atom (the α-carbon). They
are classified based on their side chain (R group) properties, including polarity, charge, and
 Unit 2: Proteins:-

nutritional requirements. General properties include high melting points, solubility in water,
and the ability to exist as zwitterions in solution.

Classification of α-Amino Acids:-

• Based on Side Chain Properties:

• Nonpolar (Hydrophobic): These amino acids have side chains that are
predominantly hydrocarbon-like, making them relatively insoluble in water. Examples
include Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Proline, and
Phenylalanine.

• Polar (Uncharged): These amino acids have side chains containing functional groups
like hydroxyl (-OH), thiol (-SH), or amide (-CONH2), which can form hydrogen bonds
and increase solubility in water. Examples include Serine, Threonine, Cysteine,
Asparagine, Glutamine, and Tyrosine.

• Acidic (Negatively Charged): These amino acids have side chains with carboxyl
groups (-COOH) that can lose a proton (H+) in solution, resulting in a negative
charge. Examples include Aspartic acid and Glutamic acid.

• Basic (Positively Charged): These amino acids have side chains with amino groups (-
NH2) that can accept a proton (H+) in solution, resulting in a positive
charge. Examples include Lysine, Arginine, and Histidine.

➢ Based on Nutritional Requirements:

• Essential Amino Acids: These amino acids cannot be synthesized by the body and
must be obtained from the diet. Examples include histidine, isoleucine, leucine,
lysine, methionine, phenylalanine, threonine, tryptophan, and valine.

• Nonessential Amino Acids: These amino acids can be synthesized by the body, so
they don't need to be obtained from the diet. Examples include alanine, asparagine,
aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, and
tyrosine.

➢ General ProPerties of α-amino acids:-

• High Melting and Decomposition Points:

➔ Unlike typical amines or organic acids, amino acids have high melting and decomposition
points, resembling those of inorganic salts. This is due to their zwitterionic nature, where the
molecule has both positive and negative charges.

• Zwitterionic Nature:

➔ At neutral pH, amino acids exist as zwitterions, where the amino group is protonated (-NH3+)
and the carboxyl group is deprotonated (-COO-).

• Amphoteric Behavior:

➔ Due to the presence of both acidic (carboxyl) and basic (amino) groups, amino acids can act
as both acids and bases, making them amphoteric.
 Unit 2: Proteins:-

• Optical Activity:

➔ Most α-amino acids are optically active (except glycine) because their α-carbon is a chiral
center (containing four different groups attached to it).

• Solubility:

➔ Amino acids are generally soluble in water due to their polar nature and ability to form
hydrogen bonds. Their solubility varies depending on the side chain's properties.

• Titration Curves:

➔ Amino acids exhibit characteristic titration curves, which show how the protonation and
deprotonation of the amino and carboxyl groups change with pH.

• Isoelectric Point (pI):

➔ The isoelectric point is the pH at which the amino acid carries no net electrical charge. At
this point, the molecule exists as a zwitterion, and its solubility is minimal.

➢ Essential and non-essential α-amino acids are vital for various bodily functions, including
protein synthesis, tissue repair, and neurotransmitter production. Essential amino acids,
which the body cannot produce, must be obtained through diet. Non-essential amino acids,
on the other hand, can be synthesized by the body. Both types play crucial roles in
maintaining overall health and well-being.

Essential Amino Acids:-

• Definition:

Essential amino acids are those that the body cannot synthesize and must be obtained from food.

• Examples:

Histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine
are considered essential amino acids.

• Physiological Importance:

• Protein Synthesis: Essential for building and repairing tissues, including muscle
mass.

• Neurotransmitter Production: Precursors for neurotransmitters in the brain,

influencing mood, sleep, and cognitive function.

• Hormone Synthesis: Involved in the production of various hormones.

• Enzyme Production: Essential for the synthesis of numerous enzymes that catalyze
biochemical reactions.

• Overall Health: Contribute to various metabolic processes and overall health.

Non-Essential Amino Acids:-

• Definition:
 Unit 2: Proteins:-

Non-essential amino acids are those that the body can synthesize from other compounds.

• Examples:

Alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline,
serine, and tyrosine are considered non-essential.

• Physiological Importance:

• Protein Synthesis: While the body can synthesize them, they are still important for
building and repairing tissues.

• Detoxification: Play a role in removing toxins from the body.

• Red and White Blood Cell Synthesis: Involved in the production of red and white
blood cells.

• Brain Function: Contribute to proper brain function and neurotransmitter synthesis.

• Other Metabolic Processes: Involved in various metabolic pathways, including

glucose metabolism and acid-base balance.

• Functional Roles: Some non-essential amino acids play specific functional roles, such
as glutamine and glutamate being metabolic fuels for the small intestine.

General imPortance:-
• Overall Health:

Both essential and non-essential amino acids are crucial for maintaining overall health and well-
being.

• Balanced Diet:

While the body can synthesize non-essential amino acids, it's important to consume a balanced diet
that provides a variety of amino acids.

• Nutritional Adequacy:

The body's ability to synthesize non-essential amino acids is dependent on an adequate supply of
essential amino acids and other nutrients.

• Functional Amino Acids:

The concept of "functional amino acids" is emerging, where both essential and non-essential amino
acids are recognized for their specific roles in regulating metabolic pathways and promoting health.

Proteins:-
➔ Protein structures are stabilized by a combination of strong and weak
bonds. Covalent bonds like peptide bonds and disulfide bonds are crucial,
while non-covalent interactions like hydrogen bonds, ionic bonds, van der
Waals forces, and hydrophobic interactions also play a significant role.
 Unit 2: Proteins:-

Here's a more detailed breakdown:

• Covalent Bonds:
• Peptide Bonds: These are the backbone of a protein, linking amino
acids together to form the polypeptide chain.
• Disulfide Bonds: Covalent bonds between cysteine residues help
stabilize the protein's structure, particularly in the tertiary and
quaternary levels.
• Non-covalent Bonds:
• Hydrogen Bonds: These are weak, but collectively contribute
significantly to the stability of protein structures, particularly in
secondary structures like alpha helices and beta sheets.
• Ionic Bonds (Salt Bridges): These electrostatic attractions between
positively and negatively charged side chains help stabilize the
protein's overall shape.
• Van der Waals Forces: These are weak, short-range attractions
between atoms due to temporary fluctuations in electron distribution.
• Hydrophobic Interactions: These are forces that drive hydrophobic
amino acid side chains to cluster together in the protein's interior, away
from water.
➢ Protein structures are made by condensation of amino acids forming peptide
bonds. The sequence of amino acids in a protein is called its primary
structure. The secondary structure is determined by the dihedral angles of the
peptide bonds, the tertiary structure by the folding of protein chains in space.
Association of folded polypeptide molecules to complex functional proteins
results in quaternary structure.

Define Protein Structure

➔ Protein structure is defined as a polymer of amino acids joined by peptide
bonds.
 Unit 2: Proteins:-

Let us see how a peptide bond is established from the following reaction:

Formation of Peptide Bond

We can thus see that the peptide bond (-CO-NH) is formed between the amine
group of one molecule and the carboxyl group of the adjacent molecule followed by
the elimination of a water molecule. This bond is otherwise an amide linkage. When
peptide bonds are established among more than ten amino acids, they together form
a polypeptide chain. Very often, when a polypeptide chain has a mass exceeding
10000u and the number of amino acids in the chain exceeding 100, we get a protein.
Classification of Proteins
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.
Levels of Protein Structure
1. Primary Structure of Protein
• The Primary structure of proteins is the exact ordering of amino acids forming
their chains.
• The exact sequence of the proteins is very important as it determines the final
fold and therefore the function of the protein.
• The number of polypeptide chains together form proteins. These chains have
amino acids arranged in a particular sequence which is characteristic of the
specific protein. Any change in the sequence changes the entire protein.
The following picture represents the primary protein structure (an amino acid chain).
As you might expect, the amino acid sequence within the polypeptide chain is crucial
for the protein’s proper functioning. This sequence is encrypted in the DNA genetic
 Unit 2: Proteins:-

code. If mutation is present in the DNA and the amino acid sequence is changed, the
protein function may be affected.

➢ The protein ‘s primary structure is the amino acid sequence in its polypeptide
chain. If proteins were popcorn stringers designed to decorate a Christmas
tree, a protein ‘s primary structure is the sequence in which various shapes
and varieties of popped maize are strung together.
➢ Covalent, peptide bonds which connect the amino acids together maintain the
primary structure of a protein.
➢ All documented genetic disorders, such as cystic fibrosis, sickle cell anemia,
albinism, etc., are caused by mutations resulting in alterations in the primary
protein structures, which in turn lead to alterations in the secondary , tertiary
and probably quarterly structure.
➢ Amino acids are small organic molecules consisting of a chiral carbon with
four substituents. Of those only the fourth the side chain is different among
amino acids.

2. Secondary Structure of Protein

Secondary structure of protein refers to local folded structures
that form within a polypeptide due to interactions between atoms of the backbone.
• The proteins do not exist in just simple chains of polypeptides.
• These polypeptide chains usually fold due to the interaction between the
amine and carboxyl group of the peptide link.
• The structure refers to the shape in which a long polypeptide chain can exist.
• They are found to exist in two different types of structures α – helix and β –
pleated sheet structures.
• This structure arises due to the regular folding of the backbone of the
polypeptide chain due to hydrogen bonding between -CO group and -NH
groups of the peptide bond.
• However, segments of the protein chain may acquire their own local fold,
which is much simpler and usually takes the shape of a spiral an extended
shape or a loop. These local folds are termed secondary elements and form
the proteins secondary structure.
 Unit 2: Proteins:-

(a) α – Helix:
α – Helix is one of the most common ways in which a polypeptide chain forms all
possible hydrogen bonds by twisting into a right-handed screw with the -NH group of each
amino acid residue hydrogen-bonded to the -CO of the adjacent turn of the helix. The
polypeptide chains twisted into a right-handed screw.
(b) β – pleated sheet:
In this arrangement, the polypeptide chains are stretched out beside one another and
then bonded by intermolecular H-bonds. In this structure, all peptide chains are stretched
out to nearly maximum extension and then laid side by side which is held together by
intermolecular hydrogen bonds. The structure resembles the pleated folds of drapery and
therefore is known as β – pleated sheet

3. Tertiary Structure of Protein

• This structure arises from further folding of the secondary structure of the protein.
• H-bonds, electrostatic forces, disulphide linkages, and Vander Waals forces stabilize
this structure.
• The tertiary structure of proteins represents overall folding of the polypeptide chains,
further folding of the secondary structure.
• It gives rise to two major molecular shapes called fibrous and globular.
• The main forces which stabilize the secondary and tertiary structures of proteins are
hydrogen bonds, disulphide linkages, van der Waals and electrostatic forces of
attraction.
 Unit 2: Proteins:-

4. Quaternary Structure of Protein

The spatial arrangement of various tertiary structures gives rise to the quaternary
structure. Some of the proteins are composed of two or more polypeptide chains referred
to as sub-units. The spatial arrangement of these subunits with respect to each other is
known as quaternary structure.

➢ The exact amino acid sequence of each protein drives it to fold into its own
unique and biologically active three-dimensional fold also known as the
tertiary structure. Proteins consist of different combinations of secondary
elements some of which are simple whereas others are more complex. Parts
of the protein chain, which have their own three-dimensional fold and can be
attributed to some function are called “domains”. These are considered
today as the evolutionary and functional building blocks of proteins.
➢ Many proteins, most of which are enzymes contain organic or elemental
components needed for their activity and stability. Thus the study of protein
evolution not only gives structural insight but also connects proteins of quite
different parts of the metabolism.
Rules of Protein Structure
• The type determines the function of a protein.
• A protein’s shape is determined by its primary structure (the amino acid
sequence).
• The amino acid sequence within a protein is determined by the encoding
sequence of nucleotides in the gene (DNA).
Summary of Protein Structure
Linderstrom-Lang (1952) in particular first suggested a hierarchy of protein structure
with four levels: central, secondary, tertiary , and quaternary. You are already familiar
with this hierarchy, because the most useful starting point for teaching basic protein
structure is this structural grouping.
• The primary structure of protein is the hierarchy’s basic level, and is the
particular linear sequence of amino acids comprising one polypeptide chain.
• Secondary structure is the next level up from the primary structure, and is
the regular folding of regions into specific structural patterns within one
polypeptide chain. Hydrogen bonds between the carbonyl oxygen and the
peptide bond amide hydrogen are normally held together by secondary
structures.
 Unit 2: Proteins:-

• Tertiary structure is the next level up from the secondary structure, and is
the particular three-dimensional arrangement of all the amino acids in a single
polypeptide chain. This structure is usually conformational, native, and active,
and is held together by multiple noncovalent interactions.
• Quaternary structure is the next ‘step up’ between two or more polypeptide
chains from the tertiary structure and is the specific spatial arrangement and
interactions.

What is Denaturation of Proteins?

➢ Denaturation implies the destruction of the tertiary structure of a protein
molecule and the formation of random polypeptide chains.
➢ Denaturation of proteins is one of the phenomenons that results in the
disturbance of stability and structure of the protein. The chemistry of proteins
has always been important owing to the abundance of these biomolecules in
the living system. The fundamental blocks of our body structure and their
functioning require protein. This protein is supplied to our body through food
products such as pulses, cheese, milk, meat, nuts, etc.
What causes Denaturation of Proteins?
➢ These biomolecules are also required for the proper maintenance of our
bodies. We have studied the different structures of proteins; it has a unique
three-dimensional structure.

The stability of protein and its structure depends on physical and chemical
conditions.

Temperature 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.
 Unit 2: Proteins:-

• 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.
Process of Denaturation of Proteins
• Secondary, tertiary and quaternary protein structure is
easily changed by a process called denaturation. These
changes can be quite damaging.
• Heating, exposure to acids or bases and even violent
physical action can cause denaturation to occur.
• The albumin protein in egg white is denatured by heating
so that it forms a semisolid mass. Almost the same thing
is accomplished by the violent physical action of an egg
beater in the preparation of meringue.
• Heavy metal poisons such as lead and cadmium change
the structure of proteins by binding to functional groups
on the protein surface.
• Denaturation of proteins can be done by bringing in
physical changes as well as the introduction of chemicals.
• Most of the denaturation processes are irreversible, but it
has been seen (in very few cases) that some of the
denaturation processes can be reversed; it is then called
as renaturation of protein.
• Some of the common cases of denaturation of proteins
are coagulation of egg white when an egg is subjected to
boiling. Here the denaturation occurs due to change in
temperature.
 Unit 2: Proteins:-

• Curdling of milk is another example of denaturation of

proteins where the formation of lactic acid by microbial
action results in denaturation.
➢ Protein is a vast subject of research in science. The development of
technology has rendered us the ability to extract so much information about
these biomolecules. Learning is a continuous process and even the scientists
keep learning new things about these biomolecules.
➢ Protein renaturation is the process where a denatured protein, which has lost
its functional shape due to factors like heat or chemicals, returns to its
original, native conformation. It's essentially the reverse of denaturation and is
crucial for restoring a protein's biological activity.

Key aspects of protein renaturation:

• Denaturation:
This is the process where proteins lose their native structure and function due to
external factors.
• Reversal of Denaturation:
Renaturation is the process of returning a denatured protein to its original, functional
shape.
• Importance:
Renaturation is vital for recovering the activity of proteins that have been unfolded,
particularly in biotechnological applications like producing recombinant proteins.
• Factors Affecting Renaturation:
Several factors can influence renaturation, including the presence of denaturants,
temperature, pH, and the protein's concentration.
• Methods of Renaturation:
Common methods include dilution, dialysis, and chromatographic techniques.
• Inclusion Bodies:
Renaturation is often necessary when proteins are produced in bacteria (like E. coli)
and form insoluble aggregates called inclusion bodies. Restoring the protein's native
structure is essential for its use.
 Unit 2: Proteins:-

➢ Proteins can be broadly classified into simple proteins and conjugated

proteins. Simple proteins are composed solely of amino acids, while
conjugated proteins consist of amino acids and additional non-amino acid
components, known as prosthetic groups. These prosthetic groups can be
carbohydrates, lipids, metal ions, phosphate groups, or nucleic acids.
Simple Proteins:
• Definition: These proteins are made up solely of amino acids linked together
by peptide bonds.
• Examples: Albumins, globulins, and histones are examples of simple
proteins.
• Hydrolysis: When simple proteins are hydrolyzed, they yield only amino
acids.
Conjugated Proteins:
• Definition:
These proteins consist of a protein component (made of amino acids) and a non-
protein component (prosthetic group).
• Examples:
Nucleoproteins (protein + nucleic acid), glycoproteins (protein + carbohydrate),
lipoproteins (protein + lipid), phosphoproteins (protein + phosphate group), and
metalloproteins (protein + metal ion) are examples of conjugated proteins.
• Prosthetic Groups:
The non-protein component, or prosthetic group, can be a variety of molecules that
contribute to the protein's function.
 Unit 2: Proteins:-

• Hydrolysis:
Hydrolyzing conjugated proteins yields both amino acids and the prosthetic group.
Key Differences:
Feature Simple Conjugated Proteins
Proteins

Composition Only amino Amino acids + non-amino acid component

acids (prosthetic group)

Examples Albumins, Nucleoproteins, glycoproteins

globulins

Hydrolysis Amino acids Amino acids and prosthetic group

Products only

immUnoGlobUlins:-
➢ Immunoglobulins (Ig), also known as antibodies, are glycoprotein molecules
produced by plasma cells that play a crucial role in the immune system. They
are Y-shaped proteins with two heavy (H) and two light (L) chains, and can be
categorized into five main classes: IgG, IgA, IgM, IgE, and IgD. Each class
has a unique structure and function, contributing to different aspects of the
immune response.
Basic Structure:

• Heavy and Light Chains:

Immunoglobulins are composed of two identical heavy chains and two identical light
chains.
 Unit 2: Proteins:-

• Constant and Variable Regions:

Each chain contains both constant and variable regions. The variable regions,
located at the tips of the "Y", are responsible for antigen binding. The constant
regions determine the antibody's class and mediate various effector functions.
• Disulfide Bonds:
The heavy and light chains are held together by disulfide bonds.
• Carbohydrate Groups:
Immunoglobulins are glycoproteins, meaning they have carbohydrate groups
attached to their chains.
• Fragments:
Antibodies can be cleaved into two functional fragments: Fab (Fragment, antigen
binding) and Fc (Fragment, crystallizable).
Classes of Immunoglobulins:
• IgG:
The most abundant antibody in serum, it provides long-term immunity and is crucial
in secondary immune responses.
• IgA:
Found in secretions like saliva, tears, and breast milk, it provides mucosal immunity.
• IgM:
The first antibody produced during an infection, it activates the complement system.
• IgE:
Involved in allergic reactions and parasitic infections, it binds to mast cells.
• IgD:
Its function is not fully understood, but it is thought to play a role in B cell activation.

Functions of Immunoglobulins:
• Antigen Binding: Immunoglobulins bind to specific antigens (e.g., bacteria,
viruses).
• Neutralization: They can neutralize toxins and pathogens.
• Opsonization: They coat pathogens, making them easier for phagocytes to
engulf.
• Complement Activation: Some classes (like IgM and IgG) can activate the
complement system, which is a part of the innate immune response.
 Unit 2: Proteins:-

• ADCC (Antibody-Dependent Cell-mediated Cytotoxicity): Certain

antibodies can bind to infected cells and trigger their destruction by immune
cells.
• Allergic Reactions: IgE mediates allergic reactions by binding to mast cells,
causing them to release histamine and other inflammatory mediators.
• Placental Transfer: IgG can cross the placenta, providing passive immunity
to the fetus.

antiGenic determinants:-
➢ Antigenic determinants on immunoglobulins (antibodies) are specific regions
of an antibody molecule that are recognized by the immune system. These
determinants can be categorized into three main types: isotypic, allotypic, and
idiotypic determinants.
• Isotypic Determinants:
These are found in the constant regions of immunoglobulin heavy and light
chains and define the antibody class (IgG, IgM, etc.) and subclass within a
species.

• Allotypic Determinants:
These are subtle amino acid differences in the heavy and light chains,
resulting from different alleles of the isotype genes. They distinguish between
individual antibodies within a species.
• Idiotypic Determinants:
These are unique to each antibody and are located in the hypervariable
regions (complementarity-determining regions, CDRs) of the heavy and light
chains. They define the antibody's binding specificity for a particular antigen.