Class 12 Chemistry Biomolecules Notes

Class 12 Chemistry Biomolecules Notes

  1. Carbohydrates
  2. Monosaccharides
  3. Glucose & Fructose
  4. Disaccharides
  5. Polysaccharides
  6. Proteins
  7. Enzymes
  8. Vitamins
  9. Nucleic Acids
  10. Hormones
  11. Chapter Summary
  12. Important Differences
  13. Exam Questions
  14. Mind Map

Part 1: Carbohydrates

Chapter Overview

Biomolecules are the chemical substances that make up living organisms. Among them, carbohydrates are the most abundant organic compounds found in nature. They are produced mainly by green plants during photosynthesis and serve as the primary source of energy for almost all living organisms.


1. What are Carbohydrates?

Definition

Carbohydrates are polyhydroxy aldehydes, polyhydroxy ketones, or compounds that produce them on hydrolysis.

They are commonly known as sugars or saccharides.

Important Point

Earlier, carbohydrates were believed to be hydrates of carbon because many have the general formula:

Cx(H₂O)y

However, this formula is not a true definition because:

  • Some compounds satisfy the formula but are not carbohydrates.
  • Some carbohydrates do not follow this formula.

Examples

CarbohydrateCommon Name
GlucoseBlood sugar
FructoseFruit sugar
SucroseCane sugar
LactoseMilk sugar
MaltoseMalt sugar
StarchPlant storage food
CellulosePlant cell wall material
GlycogenAnimal starch

Why are Carbohydrates Important?

Carbohydrates perform several essential functions.

1. Main Source of Energy

  • Glucose is the body’s preferred energy source.
  • Cells break down glucose during respiration to produce ATP.

2. Energy Storage

Plants store carbohydrates as:

Starch

Animals store carbohydrates as:

Glycogen

3. Structural Role

Cellulose forms the rigid cell wall of plants.

4. Industrial Importance

Carbohydrates are used in making:

  • Paper
  • Cotton cloth
  • Textiles
  • Wood products
  • Brewing industries

5. Biological Importance

Certain sugars like ribose and deoxyribose are components of nucleic acids (RNA and DNA).


Classification of Carbohydrates

Carbohydrates are classified according to the products formed during hydrolysis.

                Carbohydrates
                      │
      ┌───────────────┼───────────────┐
      │               │               │
Monosaccharides   Oligosaccharides  Polysaccharides

1. Monosaccharides

Definition

Monosaccharides are the simplest carbohydrates that cannot be hydrolysed into smaller carbohydrate units.

These are also called simple sugars.

Characteristics

  • Sweet in taste
  • Water soluble
  • Colourless crystalline solids
  • Reducing sugars
  • Immediate source of energy

Examples

  • Glucose
  • Fructose
  • Ribose
  • Galactose

Classification of Monosaccharides

Based on Functional Group

TypeFunctional GroupExample
AldoseAldehyde (-CHO)Glucose
KetoseKetone (>C=O)Fructose

Based on Number of Carbon Atoms

Carbon AtomsName
3Triose
4Tetrose
5Pentose
6Hexose
7Heptose

Examples

  • Ribose → Pentose
  • Glucose → Hexose
  • Fructose → Ketohexose

2. Oligosaccharides

Definition

Carbohydrates that produce 2–10 monosaccharide molecules on hydrolysis are called oligosaccharides.

The most common members are disaccharides.

Examples

  • Sucrose
  • Maltose
  • Lactose

3. Polysaccharides

Definition

Polysaccharides produce a large number of monosaccharides when hydrolysed.

Characteristics

  • Not sweet
  • Generally insoluble in water
  • High molecular weight
  • Storage and structural carbohydrates

Examples

  • Starch
  • Cellulose
  • Glycogen

Classification Based on Reducing Property

Carbohydrates are also classified as reducing and non-reducing sugars.

Reducing Sugars

These reduce:

  • Fehling’s solution
  • Tollens’ reagent

Examples:

  • Glucose
  • Fructose
  • Maltose
  • Lactose

Non-Reducing Sugars

Do not reduce these reagents.

Example:

  • Sucrose

Quick Comparison Table

PropertyMonosaccharidesOligosaccharidesPolysaccharides
HydrolysisCannot be hydrolysedGives 2–10 unitsGives many units
Sweet TasteYesUsually yesNo
SolubilityHighHighLow
Molecular SizeSmallMediumVery large
ExamplesGlucoseSucroseStarch

NCERT Important Points

✔ Carbohydrates are mainly produced by plants.

✔ Chemically, carbohydrates are polyhydroxy aldehydes or ketones.

✔ Monosaccharides are reducing sugars.

✔ Polysaccharides are also called non-sugars because they are not sweet.

✔ Starch is the storage carbohydrate of plants.

✔ Glycogen is the storage carbohydrate of animals.

✔ Cellulose is the main component of plant cell walls.


Memory Tricks

Types of Carbohydrates

MOP

  • M → Monosaccharides
  • O → Oligosaccharides
  • P → Polysaccharides

Storage Forms

Plant → Starch

Animal → Glycogen


Structural Carbohydrate

Cellulose → Cell Wall

Part 2: Monosaccharides — Glucose and Fructose

1. Glucose

Introduction

Glucose is one of the most important monosaccharides.

Common Names:

  • Blood sugar
  • Dextrose

Classification:

Glucose is:

  • A monosaccharide
  • An aldohexose
  • A reducing sugar
  • A member of the D-series

Molecular Formula:

C6H12O6C_6H_{12}O_6C6​H12​O6​

Glucose occurs naturally in:

  • Sweet fruits
  • Honey
  • Ripe grapes

It is also a basic unit of many carbohydrates such as:

  • Starch
  • Cellulose

2. Preparation of Glucose

(A) From Sucrose (Cane Sugar)

When sucrose is heated with dilute mineral acids like:

  • HCl
  • H₂SO₄

it undergoes hydrolysis and produces equal amounts of:

  • Glucose
  • Fructose

Reaction:

Sucrose + Water → Glucose + Fructose


(B) From Starch

Commercial glucose is prepared by hydrolysis of starch.

Conditions:

  • Dilute H₂SO₄
  • Temperature: 393 K
  • Pressure: 2–3 atm

Reaction:

Starch + Water → Glucose


3. Structure of Glucose

The structure of glucose was determined by studying its chemical reactions.

Evidence for Open Chain Structure


1. Molecular Formula

The molecular formula of glucose was found to be:C6H12O6C_6H_{12}O_6C6​H12​O6​

This indicates the presence of six carbon atoms.


2. Formation of n-Hexane

On prolonged heating with HI:

Glucose gives n-hexane.

Conclusion:

All six carbon atoms are arranged in a straight chain.


3. Presence of Carbonyl Group

Glucose reacts with:

  • Hydroxylamine
  • Hydrogen cyanide (HCN)

to form addition products.

Conclusion:

Glucose contains a carbonyl group (>C=O).


4. Presence of Aldehyde Group

Glucose reacts with bromine water and gets oxidised to:

Gluconic acid

Conclusion:

The carbonyl group in glucose is an aldehyde group.

Therefore glucose is an aldohexose.


5. Presence of Five Hydroxyl Groups

Glucose reacts with acetic anhydride to form:

Glucose pentaacetate

Conclusion:

Glucose contains five –OH groups.


6. Presence of Primary Alcohol Group

Oxidation of glucose with nitric acid gives:

Saccharic acid

Conclusion:

Glucose contains a primary alcoholic group.


Open Chain Structure of Glucose

According to Fischer projection:

        CHO
         |
    H — C — OH
         |
    OH— C — H
         |
    H — C — OH
         |
    H — C — OH
         |
       CH2OH

This structure explains many properties of glucose.

However, some observations could not be explained by this structure.


4. Limitations of Open Chain Structure

The open-chain structure failed to explain:

(1) Absence of Aldehyde Reactions

Although glucose contains an aldehyde group, it:

  • Does not give Schiff’s test
  • Does not form sodium bisulphite addition product

(2) No Reaction of Pentaacetate with Hydroxylamine

Glucose pentaacetate does not react with hydroxylamine.

This suggests that a free aldehyde group is absent.


(3) Existence of Two Forms

Glucose exists in two crystalline forms:

α-glucose

  • Melting point: 419 K

β-glucose

  • Melting point: 423 K

The open-chain structure cannot explain these two forms.


5. Cyclic Structure of Glucose

To explain these observations, it was proposed that glucose forms a cyclic structure.

Ring Formation

The –OH group at carbon number 5 attacks the aldehyde group at carbon number 1.

This produces a cyclic hemiacetal.

Important:

Glucose forms a six-membered ring.

This structure is called:

Pyranose Structure

because it resembles the cyclic compound pyran.


6. Anomers of Glucose

The two cyclic forms of glucose differ only in the arrangement of the –OH group at carbon-1.

Carbon-1 is called:

Anomeric Carbon

The two forms are:

α-D-Glucose

  • OH group at C-1 has one orientation

β-D-Glucose

  • OH group at C-1 has opposite orientation

These two forms are called:

Anomers

Definition:

Isomers that differ only in the configuration around the anomeric carbon are called anomers.


7. D and L Configuration of Glucose

The letters D and L represent the configuration of a molecule.

They are not related to:

  • (+) or (–) optical rotation

D-Configuration:

The –OH group on the lowest asymmetric carbon is on the right side.

L-Configuration:

The –OH group is on the left side.

Glucose has:

D-(+)-Glucose

Meaning:

  • D → Configuration
  • (+) → Dextrorotatory nature

8. Fructose

Introduction

Fructose is another important monosaccharide.

Common Name:

Fruit sugar

Sources:

  • Fruits
  • Honey
  • Vegetables

Classification:

Fructose is:

  • A monosaccharide
  • A ketohexose
  • A reducing sugar
  • A member of D-series

Molecular Formula:

C6H12O6C_6H_{12}O_6C6​H12​O6​

Fructose is written as:

D-(–)-Fructose

because it is laevorotatory.


9. Structure of Fructose

Fructose contains:

  • Six carbon atoms
  • Ketone group at carbon number 2

Therefore, it is a:

Ketohexose


Cyclic Structure of Fructose

Fructose forms a cyclic structure by reaction between:

  • C-5 hydroxyl group
  • C-2 keto group

This forms a:

Five-membered ring

called:

Furanose Structure

because it resembles furan.


Glucose vs Fructose (Important Difference)

PropertyGlucoseFructose
FormulaC₆H₁₂O₆C₆H₁₂O₆
TypeAldohexoseKetohexose
Functional groupAldehydeKetone
Carbonyl positionC-1C-2
Common nameDextroseFruit sugar
Optical natureD-(+)D-(–)
Ring structurePyranoseFuranose

Important Exam Points ⭐

Remember:

Glucose

  • Aldohexose
  • Pyranose ring
  • Six-membered cyclic structure
  • Forms α and β anomers

Fructose

  • Ketohexose
  • Furanose ring
  • Five-membered cyclic structure

Part 3: Disaccharides and Polysaccharides

1. Disaccharides

Definition

Disaccharides are carbohydrates that produce two monosaccharide molecules on hydrolysis.

They are formed when two monosaccharide units join together by a bond called:

Glycosidic Linkage


Glycosidic Linkage

Definition:

A glycosidic linkage is an oxygen bridge formed between two monosaccharide molecules by the loss of a water molecule.

Formation:

Monosaccharide + Monosaccharide → Disaccharide + Water

Example:

Glucose + Fructose → Sucrose + H₂O


Reducing and Non-Reducing Disaccharides

Disaccharides are classified according to the presence of free aldehyde or ketone groups.


1. Reducing Sugars

Definition:

Disaccharides that contain a free reducing group are called reducing sugars.

They can reduce:

  • Fehling’s solution
  • Tollens’ reagent

Examples:

  • Maltose
  • Lactose

2. Non-Reducing Sugars

Definition:

Disaccharides in which reducing groups are involved in glycosidic bond formation are called non-reducing sugars.

Example:

  • Sucrose

2. Sucrose

Introduction

Sucrose is one of the most common disaccharides.

Common Name:

Cane sugar

Sources:

  • Sugar cane
  • Sugar beet

Composition

Sucrose is made up of:

  • One molecule of α-D-glucose
  • One molecule of β-D-fructose

Hydrolysis:

Sucrose + Water → Glucose + Fructose


Glycosidic Bond in Sucrose

The linkage occurs between:

  • C-1 of α-D-glucose
  • C-2 of β-D-fructose

Because both reducing groups participate in bond formation:

➡ Sucrose is a non-reducing sugar.


Invert Sugar

Sucrose is:

  • Dextrorotatory (+)

After hydrolysis:

  • Glucose → Dextrorotatory (+)
  • Fructose → Laevorotatory (–)

Since fructose has stronger negative rotation, the mixture becomes:

➡ Laevorotatory

This hydrolysed product is called:

Invert Sugar


3. Maltose

Introduction

Maltose is a disaccharide consisting of:

Two α-D-glucose units


Linkage

The two glucose molecules are joined by:

α(1 → 4) glycosidic linkage

Meaning:

  • C-1 of first glucose joins with
  • C-4 of second glucose

Reducing Nature

The second glucose molecule has a free aldehyde group.

Therefore:

➡ Maltose is a reducing sugar.


4. Lactose

Introduction

Lactose is commonly known as:

Milk Sugar

It is found in milk.


Composition

Lactose contains:

  • β-D-galactose
  • β-D-glucose

Linkage

The bond is between:

  • C-1 of galactose
  • C-4 of glucose

Reducing Nature

A free aldehyde group can develop in glucose.

Therefore:

➡ Lactose is a reducing sugar.


Comparison of Disaccharides

PropertySucroseMaltoseLactose
Common nameCane sugarMalt sugarMilk sugar
ComponentsGlucose + FructoseGlucose + GlucoseGalactose + Glucose
Linkageα-D-glucose C1 → β-D-fructose C2α-glucose C1 → glucose C4β-galactose C1 → glucose C4
Reducing natureNon-reducingReducingReducing
SourceSugar caneBarley/maltMilk

5. Polysaccharides

Definition

Polysaccharides are carbohydrates that produce a large number of monosaccharide units on hydrolysis.

They are polymers of monosaccharides joined through glycosidic linkages.


Characteristics

  • High molecular mass
  • Generally tasteless
  • Insoluble or slightly soluble in water
  • Used mainly for storage and structural purposes

Examples:

  1. Starch
  2. Cellulose
  3. Glycogen

6. Starch

Introduction

Starch is the main storage polysaccharide of plants.

Sources:

  • Cereals
  • Roots
  • Tubers
  • Vegetables

It is the most important carbohydrate in the human diet.


Composition of Starch

Starch is made up of:

  • α-D-glucose units

It has two components:

(A) Amylose

Properties:

  • Water soluble
  • About 15–20% of starch
  • Long unbranched chain

Linkage:

α-D-glucose units joined by:

C-1 → C-4 glycosidic linkage


(B) Amylopectin

Properties:

  • Insoluble in water
  • About 80–85% of starch
  • Branched structure

Linkages:

Main chain:

C-1 → C-4 linkage

Branching:

C-1 → C-6 linkage


7. Cellulose

Introduction

Cellulose is:

  • The most abundant organic substance in plants
  • A major component of plant cell walls

Structure

Cellulose is made of:

β-D-glucose units

joined by:

β(1 → 4) glycosidic linkage


Important Point

Humans cannot digest cellulose because our digestive system lacks the enzyme required to break β-glycosidic bonds.


8. Glycogen

Introduction

Glycogen is the storage carbohydrate of animals.

It is also called:

Animal Starch


Location in Body

Glycogen is stored mainly in:

  • Liver
  • Muscles
  • Brain

Structure

Glycogen resembles amylopectin but:

  • Has more branches
  • Breaks down to release glucose when required

Starch vs Cellulose vs Glycogen

FeatureStarchCelluloseGlycogen
Found inPlantsPlantsAnimals
FunctionEnergy storageStructural supportEnergy storage
Monomerα-glucoseβ-glucoseα-glucose
Linkageα(1→4), α(1→6)β(1→4)α(1→4), α(1→6)
BranchingAmylopectin branchedNo branchingHighly branched

Part 4: Proteins — Amino Acids, Peptide Bonds and Protein Structure

1. Proteins

Introduction

Proteins are among the most important biomolecules present in living organisms.

The word protein comes from the Greek word:

“Proteios”
meaning primary or of prime importance.

Proteins are essential for:

  • Growth of the body
  • Repair of tissues
  • Maintaining body functions
  • Structural activities
  • Biological reactions

Sources of Proteins

Important sources include:

  • Milk
  • Cheese
  • Pulses
  • Peanuts
  • Fish
  • Meat

Basic Structure of Proteins

Proteins are polymers of α-amino acids.

This means:

  • Amino acids are the building blocks.
  • Many amino acids join together to form proteins.

2. Amino Acids

Definition

Amino acids are organic compounds containing:

  1. Amino group (–NH₂)
  2. Carboxyl group (–COOH)

General structure:

        H
        |
H₂N — C — COOH
        |
        R

Here:

R = side chain

The nature of the R group determines the properties of the amino acid.


Classification of Amino Acids

Amino acids are classified based on:

  1. Number of amino and carboxyl groups
  2. Ability of the body to synthesize them

A. Classification Based on Acidic and Basic Groups

1. Neutral Amino Acids

They contain:

  • One amino group
  • One carboxyl group

Example:

  • Glycine
  • Alanine

2. Acidic Amino Acids

They contain:

  • More carboxyl groups than amino groups

Examples:

  • Aspartic acid
  • Glutamic acid

3. Basic Amino Acids

They contain:

  • More amino groups than carboxyl groups

Examples:

  • Lysine
  • Arginine

B. Classification Based on Dietary Requirement

1. Essential Amino Acids

Definition:

Amino acids that cannot be synthesized by the human body and must be obtained through diet are called essential amino acids.

Examples:

  • Valine
  • Leucine
  • Lysine
  • Methionine

2. Non-Essential Amino Acids

Definition:

Amino acids that can be synthesized by the body are called non-essential amino acids.

Examples:

  • Glycine
  • Alanine

Important Amino Acids Table

Amino AcidSymbol
GlycineGly
AlanineAla
ValineVal
LeucineLeu
LysineLys
Glutamic acidGlu
Aspartic acidAsp
SerineSer
CysteineCys
MethionineMet
PhenylalaninePhe
TyrosineTyr
TryptophanTrp
HistidineHis
ProlinePro

3. Zwitter Ion Formation

Amino acids behave differently from ordinary amines and acids.

They exist mainly as dipolar ions in aqueous solution.

This form is called:

Zwitter Ion


Formation

The carboxyl group loses a proton:COOHCOO+H+-COOH \rightarrow -COO^- + H^+−COOH→−COO−+H+

The amino group accepts the proton:NH2+H+NH3+-NH_2 + H^+ \rightarrow -NH_3^+−NH2​+H+→−NH3+​

Therefore, amino acids contain:

  • Positive charge on amino group
  • Negative charge on carboxyl group

Properties of Zwitter Ions

Because of zwitterionic nature:

  • Amino acids behave like salts.
  • They have high melting points.
  • They are soluble in water.
  • They show amphoteric behaviour.

4. Optical Activity of Amino Acids

Most naturally occurring α-amino acids are optically active because their α-carbon is asymmetric.

Exception:

Glycine

Glycine is optically inactive because it has two hydrogen atoms attached to the α-carbon.

Most natural amino acids have:

L-Configuration


5. Peptide Bond / Peptide Linkage

Definition

A peptide bond is an amide linkage formed between:

  • Carboxyl group (–COOH) of one amino acid
  • Amino group (–NH₂) of another amino acid

The bond formed is:CONH-CO-NH-−CO−NH−


Formation of Dipeptide

Two amino acids combine with the elimination of water.

Example:

Glycine + Alanine → Glycylalanine + Water

The product contains two amino acids, so it is called a:

Dipeptide


Peptide Chain Classification

Number of Amino AcidsName
2Dipeptide
3Tripeptide
4Tetrapeptide
5Pentapeptide
6Hexapeptide
More than 10Polypeptide

A polypeptide chain containing more than 100 amino acids and having molecular mass above 10,000 u is generally called a protein.


6. Classification of Proteins Based on Shape

Proteins are mainly of two types:

             Proteins
                |
       ┌────────┴────────┐
       |                 |
 Fibrous proteins   Globular proteins

A. Fibrous Proteins

Structure

  • Long polypeptide chains arranged parallel to each other.
  • Stabilised by hydrogen bonds and disulphide bonds.

Properties

  • Fibre-like structure
  • Generally insoluble in water

Examples:

  • Keratin (hair, wool, silk)
  • Myosin (muscles)

B. Globular Proteins

Structure

Polypeptide chains are folded into spherical shapes.

Properties

  • Usually soluble in water

Examples:

  • Insulin
  • Albumins

7. Levels of Protein Structure

Protein structure exists at four levels:

  1. Primary structure
  2. Secondary structure
  3. Tertiary structure
  4. Quaternary structure

(1) Primary Structure

Definition:

The specific sequence of amino acids in a protein chain is called its primary structure.

Example:

Amino acid sequence:

A → B → C → D

Any change in this sequence produces a different protein.


(2) Secondary Structure

It refers to the regular folding of the polypeptide chain.

Main types:

A. α-Helix

  • Polypeptide chain twists into a right-handed spiral.
  • Stabilised by hydrogen bonding.

B. β-Pleated Sheet

  • Polypeptide chains are stretched and arranged side by side.
  • Stabilised by hydrogen bonds.

(3) Tertiary Structure

Definition:

The overall three-dimensional folding of a polypeptide chain is called tertiary structure.

It determines the final shape of the protein.

Stabilising Forces:

  • Hydrogen bonds
  • Disulphide bonds
  • Van der Waals forces
  • Electrostatic attraction

(4) Quaternary Structure

Some proteins contain two or more polypeptide chains called subunits.

The arrangement of these subunits is called:

Quaternary Structure

Example:

  • Haemoglobin

8. Denaturation of Proteins

Definition

Loss of biological activity of a protein due to changes in temperature or pH is called:

Denaturation


Causes

Physical changes:

  • High temperature

Chemical changes:

  • Change in pH

Effect

During denaturation:

Destroyed:

✔ Secondary structure
✔ Tertiary structure

Not destroyed:

✔ Primary structure


Examples

1. Boiling of Egg

Egg white protein coagulates due to denaturation.

2. Curd Formation

Milk protein changes due to lactic acid produced by bacteria.


Important Differences

Fibrous vs Globular Proteins

Fibrous ProteinsGlobular Proteins
Fibre-like shapeSpherical shape
Usually insolubleUsually soluble
Structural functionFunctional role
Example: KeratinExample: Insulin

Protein Structure Quick Revision

Amino acids
      ↓
Peptide bonds
      ↓
Polypeptide chain
      ↓
Protein structure

Primary
   ↓
Secondary
   ↓
Tertiary
   ↓
Quaternary

Part 5: Enzymes and Vitamins

1. Enzymes

Introduction

Living organisms perform thousands of chemical reactions continuously. These reactions occur under mild conditions inside the body with the help of special biological catalysts called:

Enzymes

Most enzymes are:

Globular proteins

They increase the rate of biochemical reactions without being consumed.


Characteristics of Enzymes

1. Biological Catalysts

Enzymes act as catalysts in living systems.

They:

  • Increase reaction speed
  • Remain unchanged after reaction
  • Are required in very small amounts

2. High Specificity

Enzymes are highly specific.

This means:

  • A particular enzyme works on a particular substrate.
  • It usually catalyses a particular reaction.

Example:

Maltase

It catalyses:MaltoseGlucose\text{Maltose} \rightarrow \text{Glucose}Maltose→Glucose


3. Enzyme Naming

Most enzymes are named by adding:

“-ase”

to the name of the substrate.

Examples:

EnzymeSubstrateReaction
MaltaseMaltoseMaltose → Glucose
SucraseSucroseSucrose → Glucose + Fructose

Some enzymes are named according to the reaction they catalyse.

Example:

Oxidoreductases

These enzymes carry out oxidation-reduction reactions.


2. Enzymes and Activation Energy

Activation Energy

Activation energy is the minimum energy required for a chemical reaction to occur.

Enzymes increase reaction rate by:

Reducing activation energy

They provide an easier pathway for the reaction.


Example

Hydrolysis of sucrose:

Without enzyme:

Activation energy = 6.22 kJ mol⁻¹

With enzyme sucrase:

Activation energy = 2.15 kJ mol⁻¹

Thus, enzymes make reactions faster by lowering the energy barrier.


3. Mechanism of Enzyme Action

Enzyme action can be explained by the formation of an:

Enzyme-Substrate Complex

General steps:

Enzyme + Substrate
          ↓
Enzyme-Substrate Complex
          ↓
Product + Enzyme

Important Terms

Substrate

The molecule on which an enzyme acts is called the substrate.

Active Site

The specific region of enzyme where substrate binds is called the active site.


4. Vitamins

Introduction

Vitamins are organic compounds required in:

  • Very small quantities
  • Normal growth
  • Proper functioning of the body

Their deficiency causes specific diseases.

Most vitamins cannot be synthesized by humans and must be obtained through diet.


Origin of the Term “Vitamin”

The word vitamin originated from:

Vital + Amine

Initially, scientists believed vitamins contained amino groups.

Later it was found that most vitamins do not contain amino groups.

Therefore, the letter “e” was removed and the term became:

Vitamin


Classification of Vitamins

Vitamins are classified according to their solubility.

                 Vitamins
                     |
        ┌────────────┴────────────┐
        |                         |
 Fat-soluble vitamins     Water-soluble vitamins
        |                         |
     A, D, E, K              B-group and C

1. Fat-Soluble Vitamins

Definition

Vitamins soluble in fats and oils but insoluble in water are called fat-soluble vitamins.

Examples:

  • Vitamin A
  • Vitamin D
  • Vitamin E
  • Vitamin K

Storage

They are stored in:

  • Liver
  • Fat tissues (adipose tissue)

2. Water-Soluble Vitamins

Definition

Vitamins soluble in water are called water-soluble vitamins.

Examples:

  • Vitamin B group
  • Vitamin C

Important Point

They cannot be stored in the body because they are easily removed through urine.

Exception:

Vitamin B₁₂ can be stored.


Important Vitamins, Sources and Deficiency Diseases

VitaminChemical NameSourcesDeficiency Disease
Vitamin ARetinolFish liver oil, carrots, milk, butterNight blindness, xerophthalmia
Vitamin B₁ThiamineYeast, cereals, milkBeriberi
Vitamin B₂RiboflavinMilk, eggs, green vegetablesCheilosis
Vitamin B₆PyridoxineCereals, meat, fishConvulsions
Vitamin B₁₂CobalaminMeat, fish, eggs, curdPernicious anaemia
Vitamin CAscorbic acidCitrus fruits, amla, green vegetablesScurvy
Vitamin DCalciferolSunlight, fish, egg yolkRickets, osteomalacia
Vitamin ETocopherolVegetable oilsMuscle weakness, RBC fragility
Vitamin KGreen leafy vegetablesIncreased blood clotting time

Vitamin Deficiency Diseases — Memory Tricks

Vitamin A → “A for Eyes”

Deficiency:

➡ Night blindness


Vitamin B₁ → “Beri Beri”

Deficiency:

➡ Beriberi


Vitamin C → “C for Citrus”

Deficiency:

➡ Scurvy


Vitamin D → “D for Dense Bones”

Deficiency:

➡ Rickets


Vitamin K → “K for Koagulation”

Deficiency:

➡ Increased blood clotting time


Fat-Soluble vs Water-Soluble Vitamins

Fat-SolubleWater-Soluble
A, D, E, KB group, C
Stored in bodyMostly not stored
Stored in liver and fat tissuesExcreted in urine
Excess may accumulateRegular supply needed

Part 6: Nucleic Acids — DNA, RNA and Their Functions

1. Nucleic Acids

Introduction

Nucleic acids are one of the most important biomolecules present in living organisms.

They are responsible for:

  • Storage of genetic information
  • Transfer of genetic information
  • Protein synthesis

The two major types of nucleic acids are:

  1. DNA (Deoxyribonucleic Acid)
  2. RNA (Ribonucleic Acid)

2. Chemical Composition of Nucleic Acids

Nucleic acids are polymers made up of smaller units called:

Nucleotides

A large number of nucleotides join together to form:

  • DNA
  • RNA

Structure of a Nucleotide

A nucleotide consists of three components:

1. Nitrogenous Base

It may be:

  • Purine
  • Pyrimidine

2. Pentose Sugar

It may be:

  • Ribose (in RNA)
  • Deoxyribose (in DNA)

3. Phosphoric Acid

It provides the phosphate group.


General Structure

        Nitrogenous Base
              |
              |
          Pentose Sugar
              |
              |
        Phosphate Group

3. Nucleosides

Definition

A compound containing:

  • Nitrogenous base
  • Pentose sugar

but without phosphate group is called a:

Nucleoside


Formation

Nitrogenous base + Sugar → Nucleoside

Nucleoside + Phosphoric acid → Nucleotide


Difference Between Nucleoside and Nucleotide

NucleosideNucleotide
Base + SugarBase + Sugar + Phosphate
No phosphate groupContains phosphate group
Forms part of nucleotidesBuilding unit of DNA/RNA

4. Nitrogenous Bases

Nitrogenous bases are of two types:

             Nitrogenous Bases
                    |
        ┌───────────┴───────────┐
        |                       |
     Purines              Pyrimidines

A. Purine Bases

Purines contain two fused rings.

Examples:

  • Adenine (A)
  • Guanine (G)

B. Pyrimidine Bases

Pyrimidines contain one ring.

Examples:

  • Cytosine (C)
  • Thymine (T)
  • Uracil (U)

Bases Present in DNA and RNA

BaseDNARNA
Adenine (A)
Guanine (G)
Cytosine (C)
Thymine (T)
Uracil (U)

5. DNA (Deoxyribonucleic Acid)

Introduction

DNA is the molecule responsible for storing hereditary information.

It controls:

  • Growth
  • Development
  • Reproduction
  • Characteristics of organisms

DNA is present mainly in:

  • Cell nucleus

Sugar Present in DNA

DNA contains:

Deoxyribose sugar

The absence of one oxygen atom compared with ribose gives DNA its name:

Deoxyribonucleic acid


6. Structure of DNA

The structure of DNA was proposed by:

Watson and Crick (1953)

They suggested the:

Double Helical Structure


Features of DNA Double Helix

1. Two Polypeptide-like Chains

DNA consists of two long nucleotide chains.

These chains are arranged:

  • Opposite to each other
  • In a helical manner

2. Sugar-Phosphate Backbone

The outer part of DNA contains:

  • Sugar molecules
  • Phosphate groups

These form the backbone of DNA.


3. Base Pairing

Nitrogen bases form pairs through hydrogen bonds.

Rules of base pairing:

Adenine pairs with Thymine

A=TA = TA=T

(two hydrogen bonds)

Guanine pairs with Cytosine

GCG \equiv CG≡C

(three hydrogen bonds)


4. Complementary Strands

The two strands of DNA are complementary.

This means:

If one strand contains:

A → T
G → C

the other strand will contain:

T → A
C → G


Importance of Complementary Base Pairing

It allows:

  • Accurate copying of DNA
  • Transfer of genetic information from one generation to another

7. RNA (Ribonucleic Acid)

Introduction

RNA is another important nucleic acid.

It plays a major role in:

  • Protein synthesis
  • Transfer of genetic information

Differences Between DNA and RNA

DNARNA
Contains deoxyribose sugarContains ribose sugar
Usually double-strandedUsually single-stranded
Contains thymineContains uracil
Stores genetic informationHelps in protein synthesis

Types of RNA

There are three main types:

                RNA
                 |
     ┌───────────┼───────────┐
     |           |           |
   mRNA        tRNA        rRNA

1. Messenger RNA (mRNA)

Function:

Carries genetic information from DNA to ribosomes.

It acts as a template for protein formation.


2. Transfer RNA (tRNA)

Function:

Carries amino acids to ribosomes during protein synthesis.

It helps arrange amino acids in the correct sequence.


3. Ribosomal RNA (rRNA)

Function:

It forms a major part of ribosomes.

Ribosomes are the sites where proteins are synthesized.


DNA vs RNA — Quick Comparison

FeatureDNARNA
Full formDeoxyribonucleic acidRibonucleic acid
SugarDeoxyriboseRibose
StrandsDoubleUsually single
BaseThymine presentUracil present
Main roleGenetic storageProtein synthesis

8. Biological Functions of Nucleic Acids

DNA Functions

1. Storage of Genetic Information

DNA stores hereditary information.


2. Transmission of Hereditary Characters

DNA passes information from parents to offspring.


3. Controls Protein Formation

DNA contains instructions for making proteins.


RNA Functions

1. Protein Synthesis

RNA helps in converting genetic information into proteins.


2. Transport of Amino Acids

tRNA carries amino acids during protein formation.


9. DNA Fingerprinting

Introduction

DNA fingerprinting is a technique used to identify individuals based on differences in DNA sequences.

It is useful in:

  • Crime investigations
  • Establishing biological relationships
  • Identification of individuals

Revision

Nucleic Acids
       |
 ┌─────┴─────┐
 DNA         RNA
 |            |
Genetic     Protein
storage     synthesis

Nucleotide =
Base + Sugar + Phosphate

Nucleoside =
Base + Sugar

Part 7: Hormones + Complete Chapter Revision

1. Hormones

Introduction

Hormones are chemical substances produced by endocrine glands that control and regulate various activities of the body.

They act as:

  • Chemical messengers
  • Regulators of physiological processes

Hormones are transported through blood to specific target organs where they produce their effects.


Classification of Hormones

Hormones can be broadly classified into:

                Hormones
                    |
       ┌────────────┴────────────┐
       |                         |
   Peptide Hormones        Steroid Hormones

1. Peptide Hormones

Definition

Peptide hormones are made up of amino acid chains.

Examples:

  • Insulin
  • Oxytocin
  • Vasopressin

Insulin

Source:

Produced by:

Pancreas

Function:

  • Controls blood glucose level
  • Helps cells absorb glucose from blood

Importance:

Insufficient insulin production causes:

Diabetes mellitus


2. Steroid Hormones

Definition

Steroid hormones are derived from cholesterol and contain steroid structures.

Examples:

  • Sex hormones
  • Adrenal hormones

Sex Hormones

Male Sex Hormone:

Testosterone

Function:

  • Development of male reproductive organs
  • Development of secondary sexual characteristics

Female Sex Hormones:

Estrogen and Progesterone

Functions:

  • Development of female reproductive system
  • Regulation of reproductive cycle

Protein Hormones vs Steroid Hormones

Protein HormonesSteroid Hormones
Made of amino acidsDerived from cholesterol
Water solubleLipid soluble
Example: InsulinExample: Testosterone

COMPLETE CHAPTER REVISION

Biomolecules — One Shot Summary


1. Carbohydrates

Definition

Carbohydrates are polyhydroxy aldehydes, polyhydroxy ketones, or substances that produce them on hydrolysis.


Classification

Carbohydrates

Monosaccharides
       |
Glucose, Fructose

Disaccharides
       |
Sucrose, Maltose, Lactose

Polysaccharides
       |
Starch, Cellulose, Glycogen

Important Facts

Glucose

  • Aldohexose
  • Formula: C₆H₁₂O₆
  • Exists in α and β forms
  • Forms pyranose ring

Fructose

  • Ketohexose
  • Fruit sugar
  • Forms furanose ring

Important Disaccharides

CompoundComponentsNature
SucroseGlucose + FructoseNon-reducing
MaltoseGlucose + GlucoseReducing
LactoseGalactose + GlucoseReducing

Important Polysaccharides

PolysaccharideFunction
StarchPlant storage carbohydrate
GlycogenAnimal storage carbohydrate
CellulosePlant structural material

2. Proteins

Basic Unit:

Amino acids

General structure:

      H
      |
H₂N — C — COOH
      |
      R

Peptide Bond

The bond between two amino acids:CONH-CO-NH-−CO−NH−

is called peptide linkage.


Protein Structure Levels

Primary Structure

Sequence of amino acids.

Secondary Structure

  • α-helix
  • β-pleated sheet

Tertiary Structure

Three-dimensional folding.

Quaternary Structure

Arrangement of multiple chains.


Protein Classification

Fibrous Proteins

  • Long chain structure
  • Insoluble
  • Example: Keratin

Globular Proteins

  • Spherical shape
  • Usually soluble
  • Example: Insulin

Denaturation

Loss of biological activity of protein due to:

  • Temperature change
  • pH change

Primary structure remains unchanged.


3. Enzymes

Definition

Enzymes are biological catalysts that increase the rate of biochemical reactions.


Properties

  • Mostly proteins
  • Highly specific
  • Reduce activation energy
  • Work under mild conditions

Enzyme Action

Enzyme + Substrate
        ↓
Enzyme-Substrate Complex
        ↓
Product + Enzyme

4. Vitamins

Classification

Vitamins

Fat Soluble:
A, D, E, K

Water Soluble:
B-group, C

Important Deficiency Diseases

VitaminDeficiency
ANight blindness
B₁Beriberi
B₁₂Pernicious anaemia
CScurvy
DRickets
KIncreased clotting time

5. Nucleic Acids

Types

  1. DNA
  2. RNA

Nucleotide

Contains:

  • Nitrogenous base
  • Sugar
  • Phosphate group

Nucleoside

Contains:

  • Nitrogenous base
  • Sugar

(No phosphate)


DNA

Function:

  • Stores genetic information
  • Transfers hereditary characters

Base Pairing:

A = T

G ≡ C


RNA

Types:

RNA TypeFunction
mRNACarries genetic message
tRNATransfers amino acids
rRNAForms ribosomes

Important Differences for Exams

DNA vs RNA

DNARNA
Deoxyribose sugarRibose sugar
Double strandedUsually single stranded
Thymine presentUracil present
Genetic storageProtein synthesis

Final Biomolecules Mind Map

                 BIOMOLECULES

                      |
 ------------------------------------------------
 |              |              |                |
Carbohydrates Proteins     Nucleic Acids    Vitamins
 |              |              |                |
Sugars       Amino acids      DNA/RNA        A,D,E,K
 |              |                               B,C
Energy       Peptide bonds
Storage      Protein structure