NUMS — Medical & Dental Entry Test

NUMS Biology — Biological Molecules and Enzymes (Set 1)

Take the NUMS Biology — Biological Molecules and Enzymes (Set 1): 30 multiple-choice questions (40 minutes) with instant scoring and a full answer review.…

What this test covers

Sample questions with answers

The first 5 questions of this test, with the correct answer and explanation.

  1. Q1. A student heats a sample of egg albumin to 90 °C. Which level of protein structure is LEAST likely to be disrupted by this treatment?

    • A. Tertiary structure
    • B. Secondary structure
    • C. Primary structure ✓
    • D. Quaternary structure

    Answer: C. Primary structure

    Explanation: Heat breaks hydrogen, ionic and hydrophobic interactions but not the covalent peptide bonds that hold the amino-acid sequence (primary structure) together.

  2. Q2. A disaccharide on hydrolysis yields two molecules of glucose joined originally by an α(1→4) glycosidic bond. The disaccharide is:

    • A. Maltose ✓
    • B. Lactose
    • C. Cellobiose
    • D. Sucrose

    Answer: A. Maltose

    Explanation: Maltose = glucose + glucose linked α(1→4). Cellobiose is the β(1→4) dimer; sucrose and lactose contain fructose and galactose respectively.

  3. Q3. Why can humans digest starch but not cellulose, even though both are polymers of glucose?

    • A. Starch is soluble in water while cellulose contains no glycosidic bonds
    • B. Cellulose molecules are too branched for enzymes to reach
    • C. Cellulose is made of fructose units, not glucose
    • D. Human enzymes can hydrolyse α-glycosidic bonds but not β(1→4) bonds of cellulose ✓

    Answer: D. Human enzymes can hydrolyse α-glycosidic bonds but not β(1→4) bonds of cellulose

    Explanation: Both are glucose polymers; starch has α-linkages which amylase hydrolyses, whereas cellulose has β(1→4) linkages for which humans lack cellulase.

  4. Q4. A triglyceride is formed from one glycerol and three fatty acids. How many molecules of water are released during its formation?

    • A. Three ✓
    • B. One
    • C. Two
    • D. Four

    Answer: A. Three

    Explanation: Each ester bond formed between a glycerol –OH and a fatty acid –COOH releases one water molecule; three ester bonds release three waters.

  5. Q5. Which feature best explains why phospholipids spontaneously form bilayers in water?

    • A. They contain three fatty-acid chains attached to glycerol
    • B. They are entirely non-polar molecules
    • C. They are linked by peptide bonds into long chains
    • D. They have a hydrophilic phosphate head and two hydrophobic fatty-acid tails ✓

    Answer: D. They have a hydrophilic phosphate head and two hydrophobic fatty-acid tails

    Explanation: Amphipathic phospholipids orient heads toward water and tails away from it, which naturally produces a bilayer.

The other 25 questions

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  1. Q6. In a DNA sample, 18% of the bases are adenine. What percentage of the bases are cytosine?

    • A. 64%
    • B. 18%
    • C. 32%
    • D. 36%
  2. Q7. Which statement correctly distinguishes RNA from DNA?

    • A. RNA is always double-stranded with complementary base pairing
    • B. RNA lacks phosphate groups in its backbone
    • C. RNA contains deoxyribose and thymine
    • D. RNA contains ribose and uracil, and is usually single-stranded
  3. Q8. Adding more substrate to an enzyme reaction restores the original rate of reaction in the presence of an inhibitor. The inhibitor is most likely:

    • A. An allosteric activator
    • B. Irreversible
    • C. Non-competitive
    • D. Competitive
  4. Q9. A non-competitive inhibitor is added to an enzyme-catalysed reaction. Which effect on the kinetics is expected?

    • A. Vmax increases while Km decreases
    • B. Vmax decreases while Km remains unchanged
    • C. Vmax unchanged while Km increases
    • D. Both Vmax and Km increase
  5. Q10. The rate of an enzyme reaction stops rising as substrate concentration increases further. The best explanation is that:

    • A. All active sites are occupied, so enzyme concentration has become limiting
    • B. The substrate has denatured the enzyme
    • C. The activation energy has risen
    • D. The products are destroying the substrate
  6. Q11. An enzyme from a hot-spring bacterium has an optimum temperature of 75 °C. Compared with human salivary amylase, it most likely has:

    • A. A lower activation energy requirement for denaturation
    • B. No active site
    • C. More stabilising bonds such as disulphide and ionic bonds in its tertiary structure
    • D. Only primary structure
  7. Q12. Pepsin works best at pH 2 while trypsin works best at about pH 8. If pepsin enters the duodenum, its activity falls mainly because:

    • A. Temperature in the duodenum is too low
    • B. Pepsin needs a coenzyme found only in the stomach
    • C. The change in pH alters ionic charges in the active site, changing its shape
    • D. Pepsin is digested instantly by bile
  8. Q13. Which pairing of cofactor type and example is correct?

    • A. Coenzyme — Cl⁻ ion
    • B. Activator — FAD permanently bound
    • C. Coenzyme — NAD⁺
    • D. Prosthetic group — Mg²⁺ loosely attached
  9. Q14. The induced-fit model differs from the lock-and-key model because it proposes that:

    • A. Enzymes can bind any substrate
    • B. The enzyme is used up during the reaction
    • C. The active site is rigid and exactly complementary before binding
    • D. The active site changes shape slightly on substrate binding to fit it more closely
  10. Q15. Enzymes speed up reactions by:

    • A. Lowering the activation energy needed for the reaction
    • B. Increasing the free-energy difference between reactants and products
    • C. Shifting the equilibrium towards the products
    • D. Raising the temperature of the reaction mixture
  11. Q16. In the end-product (feedback) inhibition of a metabolic pathway, the final product usually:

    • A. Binds to an allosteric site of the first enzyme and inhibits it
    • B. Activates all enzymes of the pathway
    • C. Denatures the substrate of the first enzyme
    • D. Binds to the active site of the last enzyme irreversibly
  12. Q17. A heavy-metal ion like Hg²⁺ permanently inactivates an enzyme by binding to its –SH groups. This is an example of:

    • A. Irreversible inhibition
    • B. Competitive reversible inhibition
    • C. Allosteric activation
    • D. Feedback inhibition
  13. Q18. Which bond links the monomers in each macromolecule correctly?

    • A. Fat — peptide bond; starch — phosphodiester bond
    • B. Protein — ester bond; DNA — glycosidic bond
    • C. DNA — peptide bond; glycogen — ester bond
    • D. Protein — peptide bond; polysaccharide — glycosidic bond
  14. Q19. Glycogen is a better energy store for animals than amylose mainly because glycogen:

    • A. Contains β-glycosidic bonds
    • B. Has a higher energy content per gram than fat
    • C. Is soluble and therefore osmotically active
    • D. Is highly branched, giving many ends for rapid release of glucose
  15. Q20. A fatty acid with one C=C double bond in its hydrocarbon chain is described as:

    • A. Monounsaturated
    • B. Hydrogenated
    • C. Polyunsaturated
    • D. Saturated
  16. Q21. Unsaturated fats are usually liquid at room temperature because:

    • A. They have longer chains than saturated fats
    • B. They form more hydrogen bonds between molecules
    • C. Cis double bonds create kinks that prevent tight packing of the chains
    • D. They contain no glycerol
  17. Q22. During electrophoresis at a pH equal to its isoelectric point, an amino acid does not migrate towards either electrode. This is because it:

    • A. Has lost its carboxyl group
    • B. Carries a net negative charge
    • C. Exists as a zwitterion with zero net charge
    • D. Carries a net positive charge
  18. Q23. Which interaction stabilises the α-helix of a protein?

    • A. Disulphide bridges between adjacent residues
    • B. Ionic bonds between phosphate groups
    • C. Peptide bonds between R-groups
    • D. Hydrogen bonds between C=O and N–H groups of the backbone
  19. Q24. Haemoglobin consists of four polypeptide chains. This level of organisation is called:

    • A. Tertiary structure
    • B. Primary structure
    • C. Quaternary structure
    • D. Secondary structure
  20. Q25. A single amino acid substitution (glutamic acid → valine) in the β-chain of haemoglobin causes sickle-cell disease. This shows that:

    • A. Amino acid sequence has no effect on folding
    • B. Only quaternary structure determines function
    • C. A change in primary structure can alter the final shape and function of a protein
    • D. Secondary structure is independent of R-groups
  21. Q26. Which reagent would detect the presence of reducing sugars such as glucose in a food sample?

    • A. Biuret reagent, giving a violet colour
    • B. Iodine solution, giving a blue-black colour
    • C. Sudan III, giving a red-stained layer
    • D. Benedict's solution, giving a brick-red precipitate on heating
  22. Q27. Water is an excellent coolant in living organisms primarily because of its:

    • A. Non-polar nature
    • B. Low density as a liquid
    • C. High latent heat of vaporisation
    • D. Low specific heat capacity
  23. Q28. Which of the following is a ketose sugar?

    • A. Galactose
    • B. Fructose
    • C. Glucose
    • D. Ribose
  24. Q29. An enzyme that removes a phosphate group from a substrate by adding water across the bond belongs to which class?

    • A. Isomerases
    • B. Ligases
    • C. Oxidoreductases
    • D. Hydrolases
  25. Q30. If an enzyme's coenzyme is derived from a vitamin, a dietary deficiency of that vitamin would most directly cause:

    • A. Denaturation of all proteins in the cell
    • B. Increased synthesis of the apoenzyme into a more active form
    • C. Reduced activity of the enzyme because the holoenzyme cannot form
    • D. Change in the enzyme's primary structure