Chapter 14 – Biomolecules (Detailed Notes)
14.1 Introduction
• Biomolecules are organic compounds produced by living organisms.
• They form the structural and functional basis of life.
• Major classes:
1. Carbohydrates – energy sources and structural components.
2. Proteins – building blocks and catalysts.
3. Nucleic acids – carriers of genetic information.
4. Lipids – energy storage and biological membranes.
14.2 Carbohydrates
Definition:
Carbohydrates are polyhydroxy aldehydes or ketones, or compounds that yield these
on hydrolysis.
General formula: Cₓ(H₂O)ᵧ
Classification:
1. Monosaccharides – simple sugars, can’t be hydrolyzed further.
Examples: Glucose, Fructose, Ribose.
2. Oligosaccharides – 2–10 monosaccharide units.
Examples: Sucrose, Maltose, Lactose.
3. Polysaccharides – many monosaccharides linked together.
Examples: Starch, Cellulose, Glycogen.
Monosaccharides
• Glucose (C₆H₁₂O₆): aldohexose, found in fruits and blood.
• Fructose: ketohexose, sweetest natural sugar.
• Ribose: pentose sugar, component of RNA.
• Exist in open-chain and cyclic (Haworth) forms.
• Show mutarotation due to α and β forms.
Disaccharide Components Linkage Reducing Nature
Maltose Glucose + Glucose α(1→4) Reducing
Lactose Glucose + Galactose β(1→4) Reducing
Disaccharide Components Linkage Reducing Nature
Sucrose Glucose + Fructose α(1→2) Non-reducing
Polysaccharides
• Starch: storage form in plants (amylose + amylopectin).
• Cellulose: β-glucose polymer, structural material in plants.
• Glycogen: storage form in animals (in liver & muscles).
14.3 Proteins and Amino Acids
Amino Acids
• Organic compounds containing –NH₂ and –COOH groups.
• Amphoteric → act as both acid and base → form zwitterions (H₃N⁺–CHR–COO⁻).
• Types:
o Acidic (Aspartic acid, Glutamic acid)
o Basic (Lysine, Arginine)
o Neutral (Glycine, Alanine)
Peptide Bond Formation
• Formed by condensation between –COOH of one amino acid and –NH₂ of
another.
→ –CO–NH– linkage.
Protein Structure Levels
1. Primary: sequence of amino acids.
2. Secondary: α-helix or β-sheet (H-bonding).
3. Tertiary: 3D folding of the chain.
4. Quaternary: multiple polypeptide chains combined (e.g., hemoglobin).
Denaturation: irreversible loss of structure due to heat, pH change, or chemicals.
14.4 Enzymes
• Biological catalysts (mostly proteins).
• Work through enzyme–substrate complex mechanism.
Enzyme Reaction
Amylase Starch → Maltose
Enzyme Reaction
Urease Urea → Ammonia + CO₂
Catalase H₂O₂ → H₂O + O₂
Properties:
• Highly specific.
• Work under mild conditions (optimum temperature & pH).
14.5 Nucleic Acids (DNA & RNA)
Components:
• Nucleotide = Sugar + Base + Phosphate.
• Sugars: Ribose (RNA), Deoxyribose (DNA).
• Bases:
o Purines: Adenine (A), Guanine (G)
o Pyrimidines: Cytosine (C), Thymine (T), Uracil (U)
Feature DNA RNA
Sugar Deoxyribose Ribose
Bases A, T, G, C A, U, G, C
Strands Double Single
Function Genetic code Protein synthesis
Base pairing (Watson–Crick Model):
• A = T (2 H-bonds)
• G ≡ C (3 H-bonds)
Types of RNA:
• mRNA (messenger)
• tRNA (transfer)
• rRNA (ribosomal)
14.6 Lipids
• Esters of fatty acids with glycerol.
• Saponification: fat + NaOH → soap + glycerol.
• Saturated fats: no C=C (solid).
• Unsaturated fats: contain C=C (oils).
• Functions:
o Energy reserve
o Protection and insulation
o Component of membranes
14.7 Vitamins
• Organic compounds essential in small quantities.
• Classification:
Type Examples Solubility Deficiency
Fat-soluble A, D, E, K In fats A – Night blindness; D – Rickets
Water-soluble B-complex, C In water C – Scurvy; B₁₂ – Anemia
Class Function
Carbohydrates Energy, storage, structure
Proteins Catalysis, structure, transport
Lipids Energy, insulation
Nucleic acids Genetic information
Vitamins Regulate metabolism
Enzymes Biological catalysis
Summary Points
• Biomolecules are vital for structure and function of life.
• Carbs → Energy, Proteins → Structure/Enzymes, Lipids → Storage,
Nucleic acids → Genetic code, Vitamins → Regulation.