1.
Introduction to Biomolecules
• Biomolecules are organic and inorganic molecules found in living organisms.
• Common elements: C, H, O, N, P, S.
• Based on molecular weight:
o Micromolecules: < 1000 Da (e.g., glucose, amino acids)
o Macromolecules: > 10,000 Da (e.g., proteins, nucleic acids,
polysaccharides)
• Primary Metabolites: Involved in normal growth (e.g., amino acids, sugars).
• Secondary Metabolites: Not directly involved in growth; e.g., alkaloids, pigments,
essential oils.
2. Carbohydrates (CHO)
• Definition: Polyhydroxy aldehydes or ketones, or compounds that yield them on
hydrolysis.
• Classification:
o Monosaccharides: Glucose, Fructose, Galactose.
▪ Glucose: Aldohexose; major fuel for respiration.
▪ Fructose: Ketohexose; sweetest sugar.
o Disaccharides:
▪ Sucrose: Glucose + Fructose (non-reducing)
▪ Lactose: Glucose + Galactose (reducing)
▪ Maltose: Glucose + Glucose (reducing)
o Polysaccharides:
▪ Starch: Storage in plants; made of amylose + amylopectin.
▪ Glycogen: Storage in animals (liver, muscles); highly branched.
▪ Cellulose: Structural polysaccharide in plant cell walls; not digestible
by humans.
• Bond: Glycosidic bond (C–O–C linkage).
3. Proteins (CHON, sometimes S)
• Monomers: 20 different amino acids.
• Structure of amino acid: Amino group (–NH₂), carboxyl group (–COOH), H, and R
group on α-carbon.
• Peptide bond: –CO–NH– linkage between amino acids.
• Levels of Structure:
o Primary: Linear sequence.
o Secondary: α-helix or β-pleated sheet (H-bonds).
o Tertiary: 3D structure (disulfide bridges, hydrophobic interactions).
o Quaternary: Multiple polypeptides (e.g., hemoglobin has 4 subunits).
• Types:
o Fibrous (structural): Collagen, keratin.
o Globular (functional): Enzymes, hormones.
4. Enzymes
• Biocatalysts that speed up reactions.
• Highly specific to substrate.
• Have an active site that binds substrate.
• Mechanism: "Lock and key" or "Induced fit".
• Enzyme kinetics:
o Vmax: Max reaction velocity.
o Km (Michaelis constant): [Substrate] at ½ Vmax; lower Km = higher affinity.
• Inhibition:
o Competitive: Inhibitor binds active site.
o Non-competitive: Inhibitor binds allosteric site.
• Coenzymes/cofactors:
o Coenzymes: Organic (e.g., NAD⁺, FAD).
o Cofactors: Metal ions (e.g., Mg²⁺, Zn²⁺).
5. Lipids
• Insoluble in water, soluble in organic solvents.
• Simple lipids: Fats (triglycerides = glycerol + 3 fatty acids).
• Compound lipids: Phospholipids (membranes), glycolipids.
• Derived lipids: Steroids (cholesterol, vitamin D, hormones).
• Saturated FAs: No double bonds.
• Unsaturated FAs: One or more double bonds.
• Functions: Energy storage, membrane structure, insulation.
6. Nucleic Acids (CHONP)
• Monomer: Nucleotide = Base + Sugar + Phosphate
• Nitrogenous bases:
o Purines: Adenine (A), Guanine (G)
o Pyrimidines: Cytosine (C), Thymine (T – DNA), Uracil (U – RNA)
• Sugar:
o Ribose (RNA), Deoxyribose (DNA)
• Bonds:
o Phosphodiester bond between 3'-OH of one sugar and 5'-phosphate of next.
• DNA: Double-stranded, antiparallel, complementary, double helix (Watson & Crick,
1953)
o A=T (2 H-bonds), G≡C (3 H-bonds)
• RNA: Single-stranded; types – mRNA, tRNA, rRNA
7. Vitamins & Coenzymes
• Vitamins: Organic molecules required in trace amounts.
• Water-soluble: B-complex, C
• Fat-soluble: A, D, E, K
• Act as coenzymes or precursors (e.g., NAD⁺ from niacin, CoA from pantothenic
acid).
8. Metabolism
• Metabolism = Anabolism + Catabolism
o Catabolism: Breakdown of complex molecules (e.g., glycolysis) → releases
energy.
o Anabolism: Synthesis of complex molecules (e.g., protein synthesis) →
requires energy.
• Reactions occur in metabolic pathways regulated by enzymes.
Important Bonds
Biomolecule Bond Type
Carbohydrates Glycosidic bond
Proteins Peptide bond
Lipids Ester bond
Nucleic acids Phosphodiester bond, H-bonds
NCERT Focus Points for NEET
• Structure of glucose (open & cyclic), amino acids, nucleotides.
• Enzyme action, Km, and inhibition types.
• Differences between DNA and RNA.
• Function & classification of biomolecules.
• Practice diagrams: α-D-glucose, DNA double helix, protein structures.
