Proteins: Definition, Classification, Chemistry,
Properties & Biological Importance
Dr. Naveed Ahmed
PMAS-Arid Agriculture
University, Rawalpindi
Introduction to Proteins
•Proteins are vital to all living organisms.
•They perform a wide range of functions including catalyzing
metabolic reactions, DNA replication, transporting molecules, and
responding to stimuli.
•This presentation will cover:
• What proteins are (definition and structure)
• Their classification
• Chemistry and bonding
• Physical and chemical properties
• Functions in the human body
• Their dietary importance
Definition of Proteins
•Proteins are polymers of amino acids
linked by peptide bonds.
•They are macromolecules made
primarily of carbon (C), hydrogen (H),
oxygen (O), nitrogen (N), and
sometimes sulfur (S).
•They are encoded by genes and
synthesized in cells by ribosomes.
•Example: Hemoglobin – a protein in
red blood cells that carries oxygen.
Basic Structure of Proteins
•The building blocks of proteins are amino
acids.
•Each amino acid contains:
• A central carbon atom (α-carbon)
• An amino group (-NH₂)
• A carboxyl group (-COOH)
• A hydrogen atom
• A side chain (R-group), which varies
and determines the amino acid's •Proteins are formed by
identity dehydration synthesis, joining
amino acids via peptide
bonds.
Classification Based on Composition
1.Simple Proteins – yield only amino acids on hydrolysis.
1. Examples: Albumins (egg white), Globulins (plasma
proteins)
2.Conjugated Proteins – consist of a protein and a non-
protein part (prosthetic group).
Examples: Hemoglobin (heme group), Lipoproteins (lipid
+ protein)
3.Derived Proteins – formed by partial hydrolysis or
denaturation of simple or conjugated proteins.
Examples: Peptones, Proteoses (used in microbiological
media)
Classification Based on Shape
•Fibrous Proteins:
• Long, thread-like structures.
• Insoluble in water.
• Serve structural functions.
• Examples: Collagen (connective tissue), Keratin (hair, nails),
Elastin (ligaments).
•Globular Proteins:
• Spherical and compact.
• Soluble in water.
• Function as enzymes, hormones, antibodies.
• Examples: Enzymes (amylase), Hormones (insulin),
Immunoglobulins.
Classification Based on Solubility
•Albumins: Water-soluble; coagulate on heating (e.g., egg white
protein).
•Globulins: Insoluble in pure water; soluble in dilute salt solutions (e.g.,
serum globulin).
•Prolamins: Soluble in 70% alcohol (e.g., gliadin from wheat).
•Glutelins: Soluble in dilute acids/alkalis (e.g., glutenin in wheat).
•Histones: Soluble in water; rich in basic amino acids; bind DNA.
•Scleroproteins: Insoluble in all solvents; structural proteins (e.g., collagen,
keratin).
Amino Acids – Building Blocks of
Proteins
•Essential Amino Acids: Must be obtained from
diet (e.g., lysine, leucine, methionine).
•Non-Essential Amino Acids: Can be synthesized
by the body (e.g., alanine, glutamine).
•There are 20 standard amino acids.
•Their unique R-groups determine their chemical
behavior.
•Analogy: Think of amino acids as alphabet
letters forming thousands of protein “words.”
Peptide Bond and Protein
Formation
•A peptide bond forms between the
carboxyl group of one amino acid and
the amino group of another.
•Dipeptides, tripeptides, and
polypeptides are formed as more
amino acids join.
•Proteins may contain hundreds or
thousands of amino acids.
•This bond is covalent and formed by
dehydration synthesis (removal of
water).
Levels of Protein Structure
•Primary Structure: Linear sequence of
amino acids (e.g., insulin – 51 amino acids).
•Secondary Structure: Folding into α-helix or
β-pleated sheet via hydrogen bonding.
•Tertiary Structure: 3D shape from
interactions among side chains (R-groups).
•Quaternary Structure: Multiple polypeptide
chains (subunits) combine.
• Example: Hemoglobin has 4 subunits.
Protein Folding and Stability
•Folding determines function.
•Stabilized by:
• Hydrogen bonds
• Disulfide bridges (e.g., between
cysteine residues)
• Hydrophobic interactions
• Ionic bonds
•Misfolding can lead to prion diseases
(e.g., mad cow disease) or Alzheimer’s.
•Molecular chaperones help proteins fold
correctly.
Physical Properties of Proteins
•Solubility: Globular proteins are water-soluble; fibrous proteins are not.
•Colloidal Nature: Proteins form stable colloids in water.
•Isoelectric Point (pI): pH at which protein has no net charge and is least
soluble.
•Viscosity & Elasticity: Important in muscle function (e.g., myosin, actin).
Chemical Properties of Proteins
•Biuret Test: Purple color indicates presence of peptide bonds.
•Ninhydrin Test: Blue or purple color for free amino acids.
•Xanthoproteic Test: Yellow color for proteins with aromatic rings.
•Hydrolysis: Breaks proteins into amino acids using acids, bases, or
enzymes (e.g., pepsin).
Protein Denaturation Methods of Protein
Analysis
•Denaturation = Loss of native •Electrophoresis: Separation
structure due to disruption of based on charge and size (e.g.,
bonds (not breaking peptide SDS-PAGE).
bonds).
•Chromatography: Separates
•Causes: proteins based on interactions
• Heat (boiling) with stationary/mobile phases
• pH changes (acid/base) (e.g., size-exclusion, ion-
• Heavy metals (Hg²⁺, Pb²⁺) exchange).
•Denatured proteins lose function.
•Spectrophotometry: Absorbance
•Example: Cooking an egg turns at 280 nm indicates protein
clear albumin into opaque white. presence (tryptophan, tyrosine).
Functions of Proteins Proteins in Enzymatic
in the Body Activities
1.Enzymes – Catalyze metabolic •Enzymes are highly specific
reactions (e.g., DNA polymerase). catalysts.
2.Structural – Form body
components (e.g., collagen in •Reduce activation energy of
connective tissue). biochemical reactions.
3.Transport – Carry molecules
(e.g., hemoglobin). •Examples:
4.Hormones – Chemical • Amylase: breaks down
messengers (e.g., insulin). starch
5.Immune – Defense (e.g., • Protease: breaks down
antibodies). proteins
6.Storage – Reserve amino acids • ATP synthase: makes ATP in
(e.g., ferritin stores iron). mitochondria
Structural and Functional Roles Transport and Storage
Proteins
•Collagen: Triple-helix; gives •Hemoglobin: Carries O₂; 4
strength to skin, bones, polypeptide chains.
tendons.
•Myoglobin: Stores O₂ in
•Keratin: Found in hair, nails, muscle cells.
feathers.
•Ferritin: Stores iron in liver
•Elastin: Gives elasticity to and spleen.
tissues like lungs and
arteries. •Albumin: Transports fatty
acids, drugs; maintains blood
•Structural proteins provide osmotic pressure.
scaffolding and resilience.
Hormonal and Immune Proteins in Metabolism and
Functions Homeostasis
•Buffering: Proteins maintain pH in
•Insulin: Lowers blood sugar;
blood (hemoglobin buffer
made by β-cells of pancreas.
system).
•Glucagon: Raises blood sugar.
•Osmoregulation: Albumin
regulates fluid balance across
•Antibodies (IgG, IgA, IgM):
capillaries.
Neutralize pathogens.
•Energy source: In starvation,
•Cytokines: Proteins that
muscle protein is converted to
mediate immune responses.
glucose via gluconeogenesis.
Dietary Sources and Daily
Requirements
•Animal Proteins: Complete –
contain all essential amino
acids (meat, eggs, milk).
•Plant Proteins: Often
incomplete; combinations
needed (beans + rice).
•RDA: ~0.8 g/kg body
weight/day; higher in children,
athletes, pregnant women.
Protein Deficiency Disorders
•Kwashiorkor: Protein deficiency with adequate calories – edema, hair
changes, lethargy.
•Marasmus: Deficiency in both protein and calories – severe weight loss,
muscle wasting.
•Both affect immunity, development, and increase infection risk
Importance of Proteins –
Summary
•Proteins are crucial for
structure, regulation, and
metabolism.
•No life without proteins: from
enzymes to antibodies, all are
protein-based.
•Balanced diet with sufficient
protein is vital for health and
growth.
