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Chemistry · Unit 19

Macromolecules: MDCAT Notes and MCQs

Proteins — classification

  • Polymers of α-amino acids linked by peptide (amide) bonds — condensation polymers. ≈ 20 amino acids; essential amino acids (≈ 8–10, e.g. valine, leucine, lysine, phenylalanine, tryptophan) must come from diet.
  • Amino acids exist as zwitterions (dipolar ions) — amphoteric. Glycine is the only optically inactive amino acid.
  • By composition: simple (only amino acids — albumin, globulin), conjugated (protein + prosthetic group — haemoglobin, glycoproteins, lipoproteins, nucleoproteins), derived (from hydrolysis — peptones).
  • By shape: fibrous — long, insoluble, structural (keratin of hair/nails, collagen of tendons, myosin, fibroin of silk); globular — compact, water-soluble, functional (enzymes, haemoglobin, insulin, antibodies, albumin).
  • By function: structural, enzymatic, transport, hormonal, defensive, contractile, storage.

Structure → function

Primary (sequence) determines folding into secondary (α-helix, β-sheet), tertiary and quaternary structures. Shape determines function — a single amino-acid change (glutamic acid → valine in β-chain of Hb) causes sickle-cell anaemia. Denaturation (heat, pH, heavy metals, alcohol) destroys 2°/3° structure (not peptide bonds) → loss of function (e.g. boiling an egg).

Biological & nutritional importance

  • Haemoglobin (O2 transport), insulin (glucose regulation), antibodies (defence), actin/myosin (contraction), collagen (connective tissue), fibrinogen (clotting), albumin (osmotic pressure), enzymes.
  • Dietary protein supplies amino acids for growth and repair; deficiency → kwashiorkor (protein) and marasmus (protein + calorie). Daily need ≈ 0.8–1 g per kg body mass. Sources: meat, eggs, milk, pulses.

Enzymes as biocatalysts

  • Mostly globular proteins; highly specific, efficient at body temperature and near-neutral pH; work in minute amounts; lower activation energy; regulated by inhibitors/activators.
  • Industrial uses: zymase (fermentation of glucose to ethanol), invertase (sucrose → glucose + fructose), diastase (starch → maltose), urease (urea → NH3 + CO2), proteases in detergents, rennin in cheese making.
PMDC learning outcomes for this unit
  • Proteins & enzymes: 19.1 Explain the basis of classification and structure–function relationship of proteins.
  • Proteins & enzymes: 19.2 Describe the role of various proteins in maintaining body functions and their nutritional importance.
  • Proteins & enzymes: 19.3 Describe the role of enzymes as biocatalysts.

Macromolecules MCQs with answers

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Q1
Keratin and collagen are examples of:
AConjugated proteins
BDerived proteins
CFibrous proteins
DGlobular proteins
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Answer: C (Fibrous proteins). They are insoluble structural (fibrous) proteins.
Q2
Haemoglobin is a:
AFibrous protein
BSimple protein
CDerived protein
DConjugated protein
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Answer: D (Conjugated protein). It contains the non-protein haem prosthetic group.
Q3
The bond that links amino acids in proteins is the:
AHydrogen bond
BGlycosidic bond
CEster bond
DPeptide bond
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Answer: D (Peptide bond). –CO–NH– peptide (amide) bonds join amino acids.
Q4
Denaturation of a protein destroys its:
APrimary structure
BSecondary and tertiary structure
CAmino acids
DPeptide bonds
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Answer: B (Secondary and tertiary structure). Denaturation breaks weak interactions; the amino-acid sequence remains intact.
Q5
Kwashiorkor is caused by deficiency of:
AVitamins
BProteins
CFats
DMinerals
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Answer: B (Proteins). Kwashiorkor results from severe protein deficiency.
Q6
The enzyme that converts glucose into ethanol is:
AInvertase
BDiastase
CZymase
DUrease
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Answer: C (Zymase). Zymase from yeast ferments glucose to ethanol and CO2.
Q7
Which amino acid is optically inactive?
AGlycine
BLysine
CAlanine
DValine
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Answer: A (Glycine). Glycine (R = H) has no chiral carbon.