Biomolecules
Carbohydrates, proteins, enzymes, vitamins, nucleic acids and hormones — NCERT Class 12 Chemistry Ch 10
Board Exam Tips
- →Classification of carbohydrates (mono-, di-, polysaccharides) and REDUCING vs NON-reducing sugars is a repeated MCQ.
- →Peptide bond (–CO–NH–) formation, Zwitterion structure of amino acids, and isoelectric point — high-yield concepts.
- →Distinguish α-helix and β-pleated sheet in protein secondary structure — repeats every year in 2-mark form.
- →DNA vs RNA differences: sugar (deoxyribose vs ribose), pyrimidine (T vs U), strands (double vs single). Learn table.
- →Learn one deficiency disease per vitamin: A → night blindness, B1 → beri-beri, C → scurvy, D → rickets, K → poor clotting.
📐 Formulas(9)
Molecular Formula of Glucose
Sucrose Hydrolysis (Inversion of Sugar)★ Board fav
Reducing vs Non-reducing Sugars★ Board fav
Peptide Bond Formation★ Board fav
Zwitterion (Amino Acid at Isoelectric Point)
Chargaff's Rules (Base Pairing in DNA)★ Board fav
α-Amino Acid General Structure
Michaelis-Menten Equation
| Symbol | Meaning |
|---|---|
| Reaction velocity | |
| Maximum velocity (at saturating [S]) | |
| Substrate concentration | |
| Michaelis constant |
Glycosidic Linkage Classification
✏️ Solved Examples
A DNA sample contains 20% adenine. Using Chargaff's rules, calculate the % of thymine, guanine and cytosine.
Chargaff: [A] = [T]
Explain why sucrose is called a non-reducing sugar while maltose is a reducing sugar, though both are disaccharides.
In sucrose, C-1 (anomeric C) of α-glucose is linked to C-2 (anomeric C) of β-fructose
An amino acid has pKa₁ (–COOH) = 2.34 and pKa₂ (–NH₃⁺) = 9.60. (i) Calculate its isoelectric point. (ii) Predict the direction of migration in an electric field at pH 6.0 and at pH 12.0.
Isoelectric point for a monoamino monocarboxylic acid
⚠️ Traps & Common Mistakes
- 1
Saying sucrose is a reducing sugar because glucose is.
✓Sucrose has both anomeric carbons locked in the glycosidic bond → NON-reducing. Only free anomeric –OH gives reducing behaviour.
- 2
Confusing DNA and RNA — writing thymine in RNA.
✓DNA has thymine (T); RNA replaces T with URACIL (U). Also DNA uses deoxyribose (no OH at C-2), RNA uses ribose.
- 3
Treating all polysaccharides as digestible.
✓α-1,4 linked (starch, glycogen) are digestible by humans; β-1,4 linked (cellulose) is not — humans lack the β-1,4 glucosidase enzyme.
- 4
Writing amino acid structure without the zwitterion in the solid state.
✓Solid amino acids exist as ionic zwitterions (–NH₃⁺, –COO⁻), giving them high melting points and water solubility.
- 5
Confusing primary, secondary, tertiary and quaternary protein structure.
✓Primary = amino acid sequence; secondary = local folding (α-helix, β-sheet, H-bonds); tertiary = overall 3-D shape; quaternary = assembly of multiple polypeptide subunits.
- 6
Assuming all vitamins are water-soluble.
✓A, D, E, K are FAT-soluble (stored in body, deficiency slow to appear). B-complex and C are WATER-soluble (excreted, need daily intake).
🎯 Practice Yourself
- Q1
State the difference between an α-helix and a β-pleated sheet.
- Q2
Give one example each of a monosaccharide, disaccharide, and polysaccharide.
- Q3
The isoelectric point of an amino acid is 5.5. At pH 8, will it move to the anode or the cathode?
- Q4
What is the difference between essential and non-essential amino acids? Give one example of each.
- Q5
Give two differences between DNA and RNA.
- Q6
Name the vitamins whose deficiencies cause: (a) night blindness (b) scurvy (c) rickets (d) beri-beri.
📝 Notes
Biomolecules
Chemistry of the four classes of molecules that make up living cells — carbohydrates, proteins, nucleic acids, and lipids — plus vitamins, hormones and enzymes that regulate biological processes.
Carbohydrates — the energy currency
Polyhydroxy aldehydes / ketones (or compounds that hydrolyse to them). Classified by hydrolysis:
- Monosaccharides (glucose, fructose, ribose): cannot be hydrolysed further.
- Oligosaccharides (sucrose, maltose, lactose): 2–10 monosaccharide units.
- Polysaccharides (starch, glycogen, cellulose): many monomer units in a chain.
Reducing vs non-reducing: a sugar is reducing if it has a free hemiacetal / hemiketal that can regenerate the open-chain –CHO or C=O form. Glucose, fructose, maltose, lactose reduce Tollens' / Fehling's / Benedict's reagents. Sucrose does NOT.
α vs β anomers: in cyclic pyranose form, C-1 –OH can be below (α) or above (β) the ring plane. α-D-glucose ⇌ β-D-glucose interconverts through the open chain — a process called mutarotation.
Proteins — polymers of α-amino acids
Amino acids are joined by peptide (–CO–NH–) bonds. 20 standard α-amino acids in nature; all except glycine are chiral, and all natural ones are of L-configuration. Essential amino acids must come from diet.
Four levels of protein structure:
- Primary — amino acid sequence.
- Secondary — α-helix or β-pleated sheet held by H-bonds along backbone.
- Tertiary — overall 3-D shape (globular, fibrous), stabilised by disulfide bridges, H-bonds, ionic and hydrophobic interactions.
- Quaternary — multiple polypeptide chains assembled (e.g. haemoglobin = 4 subunits).
Denaturation = loss of secondary/tertiary structure by heat, pH, urea → protein becomes biologically inactive (boiled egg).
Enzymes — biocatalysts
Enzymes are globular proteins that catalyse specific reactions with lock-and-key or induced-fit binding of substrate. Michaelis–Menten kinetics describes rate vs [S]. Small K_m ⇒ enzyme has HIGH affinity for its substrate.
Vitamins
Organic compounds required in small quantities for normal metabolism. Fat-soluble: A, D, E, K. Water-soluble: B-complex, C.
Nucleic acids — DNA and RNA
- DNA (deoxyribonucleic acid): double helix (Watson-Crick, 1953). Deoxyribose sugar, bases A, T, G, C. Stores genetic information.
- RNA (ribonucleic acid): single-stranded. Ribose sugar, bases A, U, G, C. Types: mRNA, tRNA, rRNA — carry out protein synthesis.
- Nucleotide = base + sugar + phosphate. Bases: purines (A, G, larger) and pyrimidines (C, T, U, smaller). Chargaff's rule enforces base pairing in DNA.
🔗 Related chapters
📖 Related study tips
Deep-dive articles to complement this chapter
