PROTEINS

1. Types of Proteins
Proteins are broadly classified based on their composition (simple or conjugated) or their
three-dimensional shape (fibrous or globular).

By Composition

Simple Proteins: These proteins yield only amino acids upon hydrolysis. They do not
contain any non-protein components. Examples: Albumins (egg white), globulins (in milk and
legumes), and glutelins (in wheat).

Conjugated Proteins: These proteins yield amino acids plus a non-protein component
(called a prosthetic group) upon hydrolysis. The protein part alone is called an apoprotein,
and the complete, active protein is a holoprotein.

Nucleoproteins: Prosthetic group is a nucleic acid (e.g., in ribosomes).

Glycoproteins: Prosthetic group is a carbohydrate (e.g., mucin in saliva, ovalbumin).

Lipoproteins: Prosthetic group is a lipid (e.g., HDL and LDL cholesterol carriers).

Phosphoproteins: Prosthetic group is a phosphate group (e.g., casein in milk, vitellin in

egg yolk).

Metalloproteins: Prosthetic group is a metal ion (e.g., hemoglobin-Iron, chlorophyll-

Magnesium).

By Shape (Conformation)

Globular Proteins:

Shape: Folded into a compact, roughly spherical or "globule" shape. Polypeptide chains
are intricately folded.

Structure: Have complex tertiary and often quaternary structures. Hydrophobic (non-polar)
R-groups are oriented toward the interior, while hydrophilic (polar) R-groups are on the
exterior.

Solubility: Generally soluble in water and salt solutions.

Function: Primarily functional and dynamic roles (e.g., enzymes, hormones, transport
proteins).

Food Examples: Myoglobin (meat color), casein (milk protein), albumins (egg white),
legumins (pea and bean proteins).
Fibrous Proteins:

Shape: Long, fiber-like or sheet-like structures. Polypeptide chains are arranged in

parallel.

Structure: Dominated by secondary structure (e.g., alpha-helices or beta-sheets) with

minimal tertiary folding.

Solubility: Generally insoluble in water.

Function: Primarily structural and protective roles.

Food Examples: Collagen (connective tissue in meat, forms gelatin when boiled), elastin
(ligaments in meat), keratin (hair, wool).

🧬 2. Amino Acids (AA)

Amino acids are the building blocks of proteins. All 20 common amino acids have a central
alpha-carbon (Cα) bonded to:
* An amino group (—NH₂)
* A carboxyl group (—COOH)
* A hydrogen atom (—H)
* A variable side chain (R-group), which determines the amino acid's identity and properties.

Classification by Nutritional Requirement

Essential Amino Acids (EAAs): Cannot be synthesized by the human body (or not in
sufficient amounts) and must be obtained from the diet.
The 9 EAAs: Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine,
Tryptophan, Valine.

(Mnemonic: "PVT TIM HALL")

Non-Essential Amino Acids (NEAAs): Can be synthesized by the human body.

Examples: Alanine, Aspartic Acid, Glutamic Acid, Serine.
Conditionally Essential: Become essential under certain conditions (e.g., illness, infancy).

Examples: Arginine, Cysteine, Glutamine, Glycine, Proline, Tyrosine.

Classification by R-Group (Chemical Properties)

 ● Non-Polar, Aliphatic R-Groups:
● Structure: Hydrocarbon chains (hydrophobic).
● Function: Cluster together in the interior of proteins to stabilize structure
(hydrophobic interactions).
* Examples: Glycine (Gly), Alanine (Ala), Valine (Val), Leucine (Leu), Isoleucine (Ile),
Proline (Pro).

Aromatic R-Groups:

Structure: Contain a benzene ring. Relatively non-polar (hydrophobic). Can absorb UV

light.
Examples: Phenylalanine (Phe), Tryptophan (Trp), Tyrosine (Tyr).

Acidic R-Groups (Negatively Charged):

Structure: Contain a second carboxyl group (—COOH) in their side chain. At neutral pH,
this group is deprotonated (—COO⁻), giving the AA a net negative charge.
ax. Examples: Aspartic acid (Asp), Glutamic acid (Glu).

Basic R-Groups (Positively Charged):

Structure: Contain an extra amino group in their side chain. At neutral pH, this group is
protonated (e.g., —NH₃⁺), giving the AA a net positive charge.

Examples: Lysine (Lys), Arginine (Arg), Histidine (His).

Sulfur-Containing R-Groups:

Structure: Contain a sulfur atom.

Examples: Methionine (Met): Non-polar, essential AA.

Cysteine (Cys): Polar. Its thiol (—SH) group is highly reactive and can form a disulfide
bond (—S—S—) with another cysteine, which is critical for stabilizing protein structure.

🧪 3. Properties of Amino Acids

Amphoteric Nature: Amino acids can act as both an acid (proton donor, via —COOH) and a
base (proton acceptor, via —NH₂).

Zwitterions: At neutral pH, the carboxyl group is deprotonated (—COO⁻) and the amino
group is protonated (—NH₃⁺). This results in a molecule with both a positive and a negative
charge, but no net charge.
This dipolar ion is called a zwitterion.
Solubility: Solubility in water is lowest at the isoelectric point (pI) and increases as the pH
moves away from the pI (as the molecules become net positive or net negative and repel
each other).

Stereoisomerism: All amino acids (except glycine) have a chiral alpha-carbon, meaning they
can exist as two mirror-image forms
(stereoisomers): L-isomers and D-isomers. In nature, virtually all amino acids found in
proteins are of the L-configuration.

⚡ 4. Isoelectric Point (pI)

Definition: The isoelectric point (pI) is the specific pH at which an amino acid (or protein) has
a net charge of zero.

At the pI: The molecule is in its zwitterionic form.

If pH < pI (acidic solution): The solution is rich in H⁺. The —COO ⁻ group will accept a
proton to become —COOH. The molecule will have a net positive charge (due to —NH₃⁺).

If pH > pI (basic solution): The solution is poor in H⁺. The —NH₃⁺ group will donate its
proton to become —NH₂. The molecule will have a net negative charge (due to —COO⁻).

Significance in Food:
Minimum Solubility: Proteins are least soluble at their pI because there is no net charge,
so the molecules do not repel each other and can easily aggregate and precipitate.

Food Application (Cheese): Casein (milk protein) has a pI of 4.6. To make cheese, acid
(from bacterial cultures) is added to milk. This lowers the pH from ~6.6 down to 4.6. At this
pI, the casein proteins lose their negative charge, aggregate, and precipitate out, forming the
curd.

🧱 5. Protein Structure
The function of a protein is dictated by its complex, three-dimensional shape, which is
described at four levels.

Primary (1°) Structure

Definition: The linear sequence of amino acids in the polypeptide chain. With elimination of
water
Bond: Held together by covalent peptide bonds.

Significance: This sequence dictates all higher levels of structure. A single change
(mutation) can alter the protein's entire function (e.g., sickle-cell anemia).
Secondary (2°) Structure

Definition: Local, repeating folding patterns of the polypeptide backbone.

Bond: Held together by hydrogen bonds between the C=O group of one amino acid and the
N-H group of another amino acid in the backbone.

Key Structures:
α-Helix (Alpha-Helix): A right-handed coil or spiral. Stabilized by hydrogen bonds. All
peptide bonds except the first and last

β-Pleated Sheet (Beta-Sheet): Segments of the chain lie parallel or anti-parallel to each
other, forming a rippled sheet.

Random Coil/Loops: Sections with no regular, defined structure.

Tertiary (3°) Structure

Definition: The overall three-dimensional folding of a single polypeptide chain. This is what
defines a globular or fibrous protein's shape.
Hydrophobic inside
Hydrophilic outside

Bond: Stabilized by interactions between the R-groups (side chains) of the amino acids.

Hydrophobic Interactions: Non-polar R-groups cluster in the protein's interior, away from
water.

Hydrogen Bonds: Between polar R-groups.

Ionic Bonds (Salt Bridges): Between positively charged (basic) and negatively charged
(acidic) R-groups.

Disulfide Bonds: Strong, covalent bonds between the —SH groups of two cysteine
residues.

Quaternary (4°) Structure

Definition: The arrangement and interaction of two or more separate polypeptide chains
(called subunits) to form a larger, functional protein complex.

Bond: Held together by the same R-group interactions as tertiary structure (hydrophobic, H-
bonds, ionic bonds, disulfide bonds).
Examples:
Hemoglobin: A globular protein with four subunits (two alpha, two beta).
 Collagen: A fibrous protein with three subunits twisted into a triple helix.

Protein Denaturation

Denaturation = loss of native structure of protein without breaking peptide bonds.

Secondary/tertiary structure is disrupted → protein loses its biological activity.

Caused by heat, acids, alkali, organic solvents etc.

Example: coagulation of egg white when heated.

Characteristics of Denatured Proteins

* Loss of solubility
* Loss of enzyme/hormone activity
* Loss of ability to crystallize
* Increased viscosity
* More susceptibility to proteolytic enzymes (digestible)
* Aggregation / precipitation may occur

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Renaturation

Process in which some denatured proteins regain native structure if denaturing condition is
removed.
Possible only if primary structure is intact.
Example: Ribonuclease refolding after removal of urea (classic experiment).

Denaturating Agents

Category Examples

Physical Heat, UV light, agitation (beating egg

whites)

Chemical Acids (HCl), alkali (NaOH), alcohols,

acetone, urea, detergents (SDS), heavy
metals (Hg²⁺, Pb²⁺)
Nutritive Value of Protein

Proteins supply essential amino acids which the body cannot synthesize.
1 g protein = 4 kcal energy
Needed for growth, enzyme formation, hormones, antibodies, repair and maintenance.

Animal proteins = high nutritive value (complete proteins).

Plant proteins = generally deficient in 1 or more essential amino acids (incomplete).

Digestibility & Biological Value

Digestibility: % of protein that is actually digested and absorbed from GIT.

animal proteins > plant proteins

Biological Value (BV): measures how efficiently absorbed protein is utilized for body protein
synthesis.

Protein Source BV

Egg protein (reference standard) ~100

Milk ~93

Meat ~75–80

Wheat proteins ~44

BV depends on amino acid pattern and digestibility.