C1 - MOLECULES OF LIFE

1.1 Water

Structure of Water Molecules

  • Composed of 1 O + 2 H atoms.
  • Atoms linked by covalent bonds; bond angle spreads 104.5^{\circ}.
  • Oxygen is more electronegative → polar molecule (no net charge but unequal e⁻ distribution).
    • O atom carries partial \delta^-, each H carries partial \delta^+.
  • Each molecule can form up to 4 H-bonds with neighbours.

Hydrogen Bonding & Inter-Molecular Interactions

  • \delta^+ H of one molecule attracts \delta^- O of another ⇒ hydrogen bond (weaker than covalent, yet strong enough to hold water together).
  • Consequences of polarity:
    • Attracts ions/polar solutes (hydrophilic; e.g. NaCl, sugars).
    • Repels non-polar solutes (hydrophobic; e.g. oils).

Key Properties & Biological Importance

  1. Universal / Versatile Solvent
    • Polar H₂O forms hydration shells around ions (e.g. Na⁺, Cl⁻) → dissociation & dispersion.
    • Enables biochemical reactions and transport (blood plasma, cytosol).
  2. High Specific Heat Capacity
    • Defined as heat (cal) needed to raise 1\,\mathrm g of H₂O by 1^{\circ}\mathrm C.
    • Large energy input → small \Delta T.
    • Buffers cellular & ocean temperatures; stabilises climate & internal homeostasis.
  3. High Latent Heat of Vaporisation
    • Heat required to convert 1\,\mathrm g liquid → gas.
    • Evaporative cooling (sweating, panting, bathing) removes large amounts of heat with minimal H₂O loss.
  4. Cohesion & Adhesion
    • Cohesion = H₂O–H₂O H-bonds → surface tension (pond-skaters, mosquito larvae).
    • Adhesion = H₂O attracted to other polar surfaces (xylem walls) → assists capillary rise; combined with cohesion drives transpiration stream.
  5. Maximum Density at 4^{\circ}\mathrm C
    • Ice (0^{\circ}\mathrm C) < density of liquid → floats, insulating aquatic life during winter.

1.2 Carbohydrates

Overview & Classification

  • Empirical formula (CH2O)n (C:H:O = 1:2:1).
  • Three main classes:
    1. Monosaccharides (1 sugar unit)
    2. Disaccharides (2 units)
    3. Polysaccharides (many units)

Monosaccharides

  • General traits: sweet, water-soluble, crystallisable, reducing sugars.
  • Functional groups: carbonyl (aldehyde / ketone) + multiple hydroxyls.
  • Classification criteria:
    1. Carbon skeleton size
    • Trioses (C3H6O_3): glyceraldehyde (aldose), dihydroxyacetone (ketose).
    • Pentoses (C5H{10}O_5): ribose, deoxyribose (DNA lacks O at C-2).
    • Hexoses (C6H{12}O_6): glucose (aldose), fructose (ketose), galactose.
    1. Position of carbonyl
    • Aldoses – carbonyl at chain end (e.g. glucose).
    • Ketoses – carbonyl internal (e.g. fructose).
  • Ring forms of glucose: α-glucose (−OH at C-1 below plane) vs β-glucose (−OH above).
  • Biological roles: immediate energy, precursors for larger carbs, structural components (ribose/deoxyribose in nucleotides, RuBP in photosynthesis).

Disaccharides

  • Formed via condensation (dehydration)glycosidic linkage; broken by hydrolysis.
  • Common examples:
    • Maltose = α-glucose + α-glucose (α-1→4 bond). Found in germinating barley; brewing.
    • Sucrose = α-glucose + β-fructose.
    • Lactose = β-galactose + α-glucose.
  • Formation of maltose: \text{α-Glu} + \text{α-Glu} \xrightarrow[-H_2O]{\text{condensation}} \text{Maltose}; breakdown reverse.

Polysaccharides

General properties: insoluble, colloidal, tasteless, non-crystallisable.

  1. Starch (plant storage)

    • Polymer of α-glucose.
    • Linkages: α-1→4 (linear) & α-1→6 (branch points).
    • Two fractions:
      Amylose – unbranched helix, 200–1500 residues, only α-1→4.
      Amylopectin – branched every 25–30 residues (α-1→6).
  2. Glycogen (animal storage)

    • Similar to amylopectin but more extensively branched (≈ every 8–12 residues).
    • Compact granules in liver & muscle; insoluble, osmotically inert.
  3. Cellulose (plant structural)

    • Linear β-glucose polymer with β-1→4 linkages.
    • Parallel chains H-bond → microfibrils → fibers (high tensile strength in cell walls).
    • Indigestible to humans (lack cellulase); ruminants utilise symbiotic microbes.

1.3 Lipids

General Features

  • Contain C, H, O; hydrophobic due to long non-polar C–H chains.
  • Not true polymers; diverse structures.
  • Functions: energy storage (alt to carbs), membrane components, insulation (blubber), vitamin transport, precursors of flavour/odour compounds.

Major Types

  1. Triglycerides (fats & oils)

    • 1 glycerol + 3 fatty acids linked by ester bonds (formed by condensation → release 3 H₂O).
    • Hydrolysis (lipase) regenerates glycerol + 3 FAs.
    • Fat vs Oil determined by FA saturation:
      Saturated FA: no C=C, straight chains → tight packing, solid at \sim 20^{\circ}\mathrm C (e.g. stearic, palmitic).
      Unsaturated FA: ≥1 C=C (cis) → kinks, loose packing, liquid (e.g. oleic). Classified as mono- or poly-unsaturated.
  2. Phospholipids

    • Glycerol + 2 FA tails + phosphate-containing head.
    • Amphipathic → self-assemble into bilayers; fundamental to membranes.
  3. Steroids

    • Four fused carbon rings + variable side chain.
    • Cholesterol, sex hormones, corticosteroids.

Structures in Detail

  • Fatty acid: long hydrocarbon tail (hydrophobic) + terminal carboxyl (hydrophilic) ⇒ amphiphilic.
  • Glycerol: C3H8O_3; triol able to form three ester linkages.

1.4 Proteins

Amino Acids – Basic Unit

  • General formula: central α-C bonded to H, NH₂, COOH, R (side chain).
  • At physiological pH (~7.4) exist as zwitterions ((^+NH_3) and (^-COO)().
  • Grouped by R-group properties:
    1. Non-polar (hydrophobic)
    2. Polar uncharged (hydrophilic)
    3. Acidic (−COOH in R)
    4. Basic (−NH₂ in R)

Levels of Protein Structure & Bonds

  1. Primary (1°) – linear AA sequence; peptide bonds.
  2. Secondary (2°) – regular coils/folds stabilised by H-bonds along backbone:
    • α-helix (every 4th AA; e.g. keratin).
    • β-pleated sheet (parallel strands; e.g. fibroin).
  3. Tertiary (3°) – 3-D folding via side-chain interactions:
    • Hydrophobic & van der Waals, H-bonds, ionic bonds, disulfide bridges (cys-cys).
    • Example: myoglobin (single chain + heme).
  4. Quaternary (4°) – ≥2 polypeptides assemble; same bonds as 3°.
    • Examples: collagen (3 helices), hemoglobin (α₂β₂ + four hemes).

Environmental Effects

  • Temperature >40^{\circ}\mathrm C & extreme pH disrupt non-covalent bonds → denaturation (loss of function). Sometimes reversible (renaturation).

Peptide Synthesis & Hydrolysis

  • Condensation: \text{AA}1 + \text{AA}2 \to \text{Dipeptide} + H_2O (peptide bond C-N forms).
  • Hydrolysis: reverse reaction, adding H₂O.

Protein Classification (Structure & Composition)

  • Fibrous – long, tough, insoluble; mainly 2°; structural (keratin, collagen).
  • Globular – compact, soluble, functional (enzymes, antibodies, hormones).
  • Conjugated – protein + prosthetic group (e.g. hemoglobin’s heme, glycoproteins).

1.5 Nucleic Acids (DNA & RNA)

Nucleotide – Fundamental Unit

  • Components joined by condensation:
    1. Pentose sugar – ribose (RNA) or deoxyribose (DNA; lacks O at C-2).