Chapter 14 — Biomolecules Exercise Solutions
Biomolecules is scoring when classification and examples are memorised clearly. Use tables to organise the information.
Key Concepts Quick Recap
| Biomolecule | Monomer | Bond | Function |
|---|
| Carbohydrates | Monosaccharides | Glycosidic bond | Energy source, cell walls, DNA backbone |
| Proteins | Amino acids | Peptide bond (amide) | Enzymes, structure, transport, immunity |
| Nucleic acids (DNA/RNA) | Nucleotides | Phosphodiester bond | Genetic information, protein synthesis |
| Lipids | Fatty acids + glycerol | Ester bond | Energy storage, membranes, hormones |
| Vitamins | Small organic molecules | — | Coenzymes, essential metabolic functions |
Carbohydrate Classification
| Type | Definition | Examples |
|---|
| Monosaccharide | Cannot be hydrolysed; single sugar unit | Glucose, fructose, galactose, ribose |
| Disaccharide | 2 monosaccharides; hydrolysed to 2 monomers | Sucrose, maltose, lactose |
| Oligosaccharide | 3–10 monosaccharides | Raffinose (3 units) |
| Polysaccharide | 100s–1000s of units | Starch, cellulose, glycogen |
Important Vitamin Table
| Vitamin | Chemical Name | Deficiency Disease | Solubility |
|---|
| A | Retinol | Night blindness, xerophthalmia | Fat |
| B₁ | Thiamine | Beriberi | Water |
| B₂ | Riboflavin | Cheilosis | Water |
| B₃ | Niacin | Pellagra | Water |
| B₁₂ | Cyanocobalamin | Pernicious anaemia | Water |
| C | Ascorbic acid | Scurvy | Water |
| D | Calciferol | Rickets (children), Osteomalacia (adults) | Fat |
| E | Tocopherol | Infertility, haemolysis | Fat |
| K | Phylloquinone | Impaired blood clotting | Fat |
I. Choose the Best Answer (MCQs)
1. Glucose is classified as: (a) Disaccharide (b) Ketohexose (c) Aldohexose (d) Aldopentose
Answer(c) Aldohexose Glucose has 6 carbons (hexose) and an aldehyde functional group (−CHO) → aldohexose. Fructose is a ketohexose (has a ketone group at C-2).
2. The peptide bond in proteins is: (a) −NH−CO− (amide bond) (b) −O−CO− (ester bond) (c) −S−S− (disulphide) (d) −O−O− (peroxide)
Answer(a) −NH−CO− (amide bond) Peptide bond forms between the −COOH of one amino acid and the −NH₂ of another: −CO−NH− (water is eliminated).
3. Which of the following is a non-reducing sugar? (a) Glucose (b) Maltose (c) Sucrose (d) Lactose
Answer(c) Sucrose In sucrose, both the anomeric carbons of glucose and fructose are involved in the glycosidic bond → no free −CHO or ketone group → non-reducing.
4. The base present in DNA but NOT in RNA is: (a) Adenine (b) Guanine (c) Cytosine (d) Thymine
Answer(d) Thymine DNA bases: A, G, C, T. RNA bases: A, G, C, U (Uracil replaces Thymine). Sugar: deoxyribose in DNA, ribose in RNA.
5. Which of the following is a fat-soluble vitamin? (a) Vitamin C (b) Vitamin B₁₂ (c) Vitamin D (d) Vitamin B₂
Answer(c) Vitamin D Fat-soluble vitamins: A, D, E, K. Water-soluble: B-complex, C. Fat-soluble vitamins are stored in the body; excess can cause toxicity.
6. Enzymes are: (a) Inorganic catalysts (b) Lipid-based catalysts (c) Protein-based biological catalysts (d) Nucleic acid catalysts
Answer(c) Protein-based biological catalysts Most enzymes are proteins (some are ribozymes — RNA-based). They are highly specific, work at mild conditions, and can catalyse reactions 10⁶ to 10¹⁷ times faster than uncatalysed.
7. The secondary structure of protein is maintained by: (a) Peptide bonds (b) Disulphide bridges (c) Hydrogen bonds (d) van der Waals forces
Answer(c) Hydrogen bonds Secondary structure (α-helix, β-pleated sheet) is maintained by hydrogen bonds between C=O and N−H groups of the peptide backbone. Peptide bonds maintain the primary structure.
II. Short Answer Questions
Q1. Classify carbohydrates with examples. What are reducing sugars?
Answer
Classification:
- Monosaccharides: single unit, cannot be hydrolysed. Example: glucose, fructose.
- Disaccharides: two monosaccharide units linked by glycosidic bond. Example: sucrose (glucose + fructose), maltose (glucose + glucose), lactose (glucose + galactose).
- Polysaccharides: many monosaccharide units. Example: starch (storage in plants), glycogen (storage in animals), cellulose (structural in plants).
Reducing sugars: Carbohydrates that can reduce Fehling's or Tollens' reagent — they have a free aldehyde or ketone group.
- Reducing: glucose, fructose, maltose, lactose.
- Non-reducing: sucrose (both anomeric carbons locked in glycosidic bond).
Q2. Describe the four levels of protein structure.
Answer
| Level | Description | Stabilised by |
|---|
| Primary | Sequence of amino acids in the polypeptide chain | Peptide (covalent) bonds |
| Secondary | α-helix or β-pleated sheet (local folding) | Hydrogen bonds |
| Tertiary | 3D folding of the polypeptide chain | H-bonds, ionic bonds, hydrophobic interactions, disulphide bridges |
| Quaternary | Association of two or more polypeptide chains | Same as tertiary |
Example: Haemoglobin has quaternary structure (2α + 2β subunits). Insulin has disulphide bridges stabilising tertiary structure.
Q3. Compare DNA and RNA.
Answer
| Feature | DNA | RNA |
|---|
| Sugar | Deoxyribose | Ribose |
| Bases | A, G, C, T | A, G, C, U |
| Strands | Double-stranded (usually) | Single-stranded (usually) |
| Location | Nucleus (mainly) | Nucleus + cytoplasm |
| Stability | More stable | Less stable |
| Function | Stores genetic information | Protein synthesis (mRNA, tRNA, rRNA) |
| Winding | Right-handed B-helix | Various secondary structures |
Base pairing in DNA: A=T (2 H-bonds), G≡C (3 H-bonds).
Q4. Write the functions of proteins with examples.
Answer
| Function | Example |
|---|
| Enzyme | Amylase, pepsin, trypsin |
| Structural | Collagen (connective tissue), keratin (hair, nails) |
| Transport | Haemoglobin (O₂), serum albumin |
| Hormones | Insulin, glucagon |
| Immune protection | Antibodies (immunoglobulins) |
| Muscle contraction | Actin, myosin |
| Storage | Casein (milk), ferritin (iron) |
Worked Examples
Example 1 — Classifying carbohydrates
Monosaccharide: Glucose (C₆H₁₂O₆) — aldohexose
Fructose (C₆H₁₂O₆) — ketohexose
Ribose (C₅H₁₀O₅) — aldopentose (backbone of RNA)
Deoxyribose (backbone of DNA)
Disaccharide: Sucrose = Glucose + Fructose (non-reducing)
Maltose = Glucose + Glucose (reducing)
Lactose = Glucose + Galactose (reducing; present in milk)
Polysaccharide: Starch — storage in plants; α-glucose units
Cellulose — structural; β-glucose units (not digested by humans)
Glycogen — storage in animals (liver, muscle)
Example 2 — Reducing vs non-reducing sugars
Test: Fehling's solution (gives brick-red Cu₂O ppt) or Tollens' reagent (silver mirror)
Reducing sugars (positive test):
Glucose, fructose, maltose, lactose ✓
Non-reducing sugar (negative test):
Sucrose — both anomeric carbons engaged in glycosidic bond; no free −CHO ✗
After hydrolysis: sucrose → glucose + fructose → both are reducing
Invert sugar = mixture of glucose + fructose obtained by hydrolysis of sucrose
Example 3 — DNA bases and complementary base pairing
DNA double helix — Chargaff's rules:
%A = %T and %G = %C
Base pairs:
A (Adenine) pairs with T (Thymine) → 2 hydrogen bonds
G (Guanine) pairs with C (Cytosine) → 3 hydrogen bonds
If one strand of DNA is: 5'−ATGCCG−3'
Complementary strand: 3'−TACGGC−5'
RNA bases replace T with U:
mRNA transcribed: 5'−AUGCCG−3'
Example 4 — Vitamin deficiency diseases
Memorise this table:
A → Night blindness (inability to see in dim light)
B₁ → Beriberi (nervous system damage)
B₂ → Cheilosis (cracks at corner of mouth)
B₃ → Pellagra (3D: Dermatitis, Diarrhoea, Dementia)
B₁₂ → Pernicious anaemia (impaired red blood cell production)
C → Scurvy (bleeding gums, poor wound healing)
D → Rickets in children, Osteomalacia in adults (bone softening)
E → Haemolysis, reproductive problems
K → Impaired blood clotting (haemorrhage)
Example 5 — Enzyme specificity
Lock-and-key model (Emil Fischer, 1890):
- The active site of an enzyme has a specific shape (the "lock").
- Only a substrate with complementary shape (the "key") can bind.
- Enzyme–substrate complex forms → reaction occurs → products released → enzyme recycled.
Induced fit model (Koshland):
- Active site is flexible and adjusts its shape when substrate approaches.
- More accurate for most enzymes.
Examples of enzyme specificity:
Urease: only hydrolyses urea → NH₃ + CO₂
Amylase: only hydrolyses starch (α-1,4 glycosidic bonds)
Pepsin: cleaves peptide bonds in acidic stomach conditions only
Answer Pattern
1. Define the biomolecule. 2. State its classification. 3. Give one specific function. 4. Give one example with a real context.
Common Mistakes
- Confusing reducing and non-reducing sugars — sucrose is non-reducing.
- Mixing DNA and RNA bases — thymine is only in DNA; uracil only in RNA.
- Saying all vitamins are water-soluble — A, D, E, K are fat-soluble.
- Vague vitamin functions — always mention the deficiency disease.
- Confusing secondary structure (H-bonds) with primary structure (peptide bonds).
Exam Checklist
- Biomolecule classification is correct.
- Examples are valid (not generic).
- Vitamin deficiency disease is paired correctly.
- DNA/RNA comparison covers bases, sugar, and strand structure.
- Protein structure levels are described in order (1° → 4°).