Biological Molecules
1. Biological Molecules — Overview
4 most common elements in living organisms: Carbon, Hydrogen, Oxygen, Nitrogen (C H O N). Other elements (Fe, Zn, Mg …) = micronutrients — needed in tiny amounts only.
| Biological molecule | Elements | Note |
|---|---|---|
| ① Carbohydrates | C, H, O | direct energy source (→ glucose → ATP) |
| ② Proteins | C, H, O, N | growth & development, enzymes, hormones |
| ③ Lipids | C, H, O | NOT a polymer — only a macromolecule |
| ④ Nucleic acids | C, H, O, N, P | RNA and DNA (studied in Ch. 6 – protein synthesis & DNA) |
| ⑤ Water | H₂O | 70–95 % of cell mass; body ≈ 60–65 % water |
Carbs → broken to glucose → oxidised → ATP (energy currency of the cell). DNA = identity card of the cell: stores hereditary info; DNA & RNA are used to make protein enzymes / protein hormones. ~90 % of blood plasma is water.
Three key terms
Macromolecule: a giant (large) molecule made up of simpler molecules. (macro = large, micro = small)
Polymer: a large molecule made up of small repeating units called monomers. (poly = many)
Monomer: a small molecule which is the repeating unit of a polymer.
2. Carbohydrates (C – H – O)
All carbohydrates contain only carbon, hydrogen and oxygen. The “hydrate” part of the name = water: H and O are present in a 2 : 1 ratio (like in H₂O).
Old idea: chemists thought carbs were “hydrates of carbon” (carbon + water molecules) — they are not actually joined with water, but the name and formula stayed. e.g. glucose C₆H₁₂O₆ → simplest ratio CH₂O.
Carbohydrates are divided into 3 main groups (saccharide = sugar / sweet):
- Monosaccharide formula (CH₂O)ₓ: hexose x = 6 → C₆H₁₂O₆; pentose x = 5 → C₅H₁₀O₅ (ribose).
- Deoxyribose = ribose with one oxygen less → C₅H₁₀O₄ (like deoxygenated blood has less O₂).
- Disaccharide: 2 monosaccharides joined by a covalent bond, 1 H₂O lost = condensation reaction (two units join → bigger unit + small molecule lost; anabolic).
- Polysaccharide = polymer ⇒ the monomers must be the same repeating unit (disaccharides can have 2 different monosaccharides, e.g. sucrose).
3. Monosaccharide — Glucose (α & β)
Glucose is made in photosynthesis and oxidised for energy → very important in exams (both forms!). In solution the straight-chain form is not stable, so it folds into a ring: C5 bonds with C1 (ring closes through O), and C6 (CH₂OH) sits outside the ring. Each C makes 4 bonds (tetravalent).
α → OH below the ring | β → OH above the ring
Important: in MCQs you must identify whether a disaccharide’s monomers are α or β glucose from the OH position; in drawing questions 1 mark is for the correct ring — drawing β instead of α loses the mark. Practise drawing both rings by heart!
4. Disaccharides (Condensation Reactions)
Formed by the joining of 2 monosaccharides with loss of 1 H₂O (condensation).
| Disaccharide | Made of | Bond |
|---|---|---|
| ① Maltose | α-glucose + α-glucose | α-1,4 glycosidic |
| ② Sucrose | α-glucose + fructose | glycosidic (C1 of glucose – C2 of fructose) |
| ③ Lactose | α-glucose + galactose or β-glucose + galactose | glycosidic |
| ④ Cellobiose | β-glucose + β-glucose | β-1,4 glycosidic |
After water is lost, O and C each have an incomplete valency, so the O bridges the two carbons. Both –OH must lie in the same plane; if not, one ring is flipped (see cellobiose). The bond is always between C1 of one and C4 of the other glucose.
Fructose — ring form
Fructose is a ketose (C=O in the middle, C2), a hexose like glucose and galactose.
Sucrose = α-glucose + fructose
Lactose
Lactose = glucose + galactose; it can be made with α-glucose + galactose or β-glucose + galactose (two forms) — joined by a glycosidic bond after loss of H₂O. (Milk sugar.)
Cellobiose = β-glucose + β-glucose
Here a problem: in β-glucose the C1 –OH points up but the C4 –OH of the other β-glucose points down, so the two –OH are not in the same plane and cannot meet. Fix: one β-glucose rotates / flips by 180° — then the C1–OH and C4–OH face each other, H₂O is lost and a β-1,4 glycosidic bond forms.
5. Reducing Sugars & Benedict’s Test
Reducing sugars (= reducing agents) can carry out reduction of another substance; in the process the sugar itself is oxidised.
- Reducing sugars = all monosaccharides + some disaccharides (maltose, lactose, cellobiose).
- Sucrose is NOT a reducing sugar (non-reducing disaccharide).
- Polysaccharides (starch, glycogen, cellulose) = non-reducing.
Benedict’s test
Benedict’s reagent = copper(II) sulfate (CuSO₄) in alkaline solution; blue colour. Reducing sugars reduce the soluble blue Cu²⁺ to insoluble brick-red copper oxide (contains Cu⁺).
Method: ① ~2 cm³ of test solution ② add an equal volume of Benedict’s solution ③ heat in a water bath ④ look for the colour change → brick-red precipitate = reducing sugar present.
Testing for a non-reducing sugar (sucrose)
Sucrose → no change with Benedict’s (stays blue) → hydrolyse with dilute HCl (boil) → breaks glycosidic bond → 2 monosaccharides (glucose + fructose = reducing sugars) → then do Benedict’s again → brick-red ppt.
6. Polysaccharides
Made by joining many monosaccharide molecules (monomers) by condensation. Examples: starch, glycogen, cellulose — all non-reducing and osmotically inactive.
Each time 2 monosaccharides join, 1 H₂O is lost, so the polysaccharide formula has 2 H and 1 O less per unit (C₆H₁₂O₆ → C₆H₁₀O₅). For n monosaccharides, (n − 1) water molecules are lost. (n = number of monosaccharides joining.)
Why store glucose as a polysaccharide?
Glucose is a reactive molecule — it would interfere with normal cell chemistry — and it is osmotically active: dissolved glucose (solute) raises the solute concentration → water potential falls → water enters by osmosis, disturbing the cell. So glucose is converted by condensation into a storage polysaccharide:
Starch (made of α-glucose) — amylose + amylopectin
| Amylose | Amylopectin | |
|---|---|---|
| Monomer | α-glucose | α-glucose |
| Shape | helical, unbranched | branched, non-helical |
| Bonds | α-1,4 glycosidic only | α-1,4 and α-1,6 |
| Digestion (hydrolysis) | more resistant (few free ends) | less resistant — more free ends because of branching |
| Mᵣ | relatively lower (fewer monomers) | relatively greater |
| Solubility | — | more water-soluble |
| With iodine solution | stains blue-black (red-brown → blue-black) | does not cause the same colour change |
Glycogen
- Monomer: α-glucose; storage polysaccharide in animal and fungal cells (granules).
- Structure is similar to amylopectin.
| Similarities with amylopectin | Differences with amylopectin |
|---|---|
| • branched • α-1,4 and α-1,6 glycosidic bonds |
• more branching in glycogen • Mᵣ greater than amylopectin • glycogen is less resistant to digestion (easier to hydrolyse) than amylopectin |
amylose (most resistant · hardest to digest) → amylopectin → glycogen (least resistant · easiest to digest). More branches = more free ends for enzymes.
Cellulose (made of β-glucose)
- Structural role — mechanically strong; found in the plant cell wall; most abundant organic molecule.
- Monomer: β-glucose; β-1,4 glycosidic bonds; general formula (C₆H₁₀O₅)ₙ (n = number of monosaccharides joined).
Cellulose molecule = linear, unbranched chain of β-glucose where every alternate β-glucose is rotated by 180° (so that C1-OH and C4-OH can meet).
Comparing polysaccharides
| Feature | Amylose | Amylopectin | Glycogen | Cellulose |
|---|---|---|---|---|
| Monomers | α-glucose | α-glucose | α-glucose | β-glucose |
| Bonds | 1,4 GB | 1,4 & 1,6 GB | 1,4 & 1,6 GB | β-1,4 GB |
| H-bonds present | ✓ | ✓ | ✓ | ✓ (key feature) |
| Structure | helical, unbranched | branched, non-helical | branched, non-helical (more branched) | linear, unbranched |
| Found in | plants | plants | animals / fungi | plants (cell wall) |
| Exists as | starch grains | starch grains | glycogen granules | fibres |
| Rotation of monomers | ✗ | ✗ | ✗ | ✓ (alternate 180°) |
| Stains with iodine | ✓ | ✗ | ✗ | ✗ |
| Role | energy store | energy store | energy store | structural |
| Reducing sugar | ✗ | ✗ | ✗ | ✗ |
| Osmotically active | ✗ | ✗ | ✗ | ✗ |
7. Lipids (C – H – O)
Fats (animal lipids) → usually solid at room temp · Oils (plant lipids) → usually liquid at room temp.
- A macromolecule but NOT a polymer — not made of repeating units of the same molecule/atoms.
- Organic compounds insoluble in water, soluble in organic solvents.
- Most lipids are formed by fatty acids combining with an alcohol.
① Triglycerides
= 3 fatty acids + 1 glycerol. Fatty acid = organic acid with a –COOH group and a long C–H chain. Glycerol (C₃H₈O₃) = trihydroxy alcohol (3 –OH groups in 1 molecule).
Fatty acids: saturated vs unsaturated
- Saturated (C–C only) · unsaturated (C=C): one double bond = monounsaturated; more than one = polyunsaturated.
- Note: double bonds make fatty acids / lipids melt more easily (loose packing).
- Skeletal formulae: C and H are not shown unless in a group (e.g. –COOH, –CH₃); each corner/end = a carbon. A 12-carbon fatty acid = 12 corners with –COOH at one end.
② Phospholipids
Amphipathic — has both a polar and a non-polar part: phosphate head = hydrophilic (water-loving), soluble; 2 fatty acid tails = hydrophobic (water-hating), insoluble. Fatty acids are joined to glycerol by ester bonds. They form membranes.
Functions / benefits of lipids (stored in adipose tissue)
- Excellent energy store — stored in unlimited amounts (kidney, under the skin, heart …).
- Many C–H bonds (energy-rich) ⇒ yield more energy than carbohydrates on oxidation of the same mass (more than 2×).
- Thermal insulation (under the skin).
- Metabolic source of water to small organisms in dry areas — aerobic respiration releases H₂O; more H atoms ⇒ more water produced.
- Synthesis of steroidal (lipid-based) hormones — testosterone, oestrogen, progesterone (control & coordination).
- Electrical insulation via the myelin sheath — prevents leakage of ions as they move across neurons.
8. Proteins (made of amino acids)
Structure of an amino acid (building block)
Peptide bond (condensation)
–COOH of one amino acid + –NH₂ of the next → –H₂O → peptide bond (–CO–NH–). 2 amino acids = dipeptide; many = polypeptide.
Levels of protein folding
① Primary structure: the sequence of amino acids in a polypeptide chain (held by peptide bonds). Decided by the DNA / gene — always the same for a given protein.
② Secondary structure: regular folding of the polypeptide chain into an α-helix or β-pleated sheet, due to hydrogen bonding between amino acids in the chain: the O of C=O of one amino acid and the H of N–H of another interact via H-bonding ⇒ chain bends back on itself.
R groups (decide tertiary structure)
| R group type | Charge | Interaction formed |
|---|---|---|
| Polar | partial charge (δ+ / δ–) | hydrogen bonds |
| Charged | complete (full) charge, + or – | ionic bonds |
| Non-polar | no charge | hydrophobic interactions (water-hating groups cluster together away from water) |
| 2 cysteines (–SH) | — | disulfide linkage (S–S) after 2 H are lost |
③ Tertiary structure: regular 3D folding of a polypeptide chain due to H-bonds (between polar R groups), hydrophobic interactions (non-polar R groups), ionic bonds (charged R groups) and disulfide linkages (between 2 cysteine R groups). Level of folding > secondary.
hydrophobic interactions < hydrogen bonds < ionic bonds < covalent bonds (disulfide + peptide). In diagrams: dotted line = weak bond; straight line = strong permanent bond.
④ Quaternary structure: forms when 2 or more polypeptide chains (of a protein) associate via H-bonds, hydrophobic interactions, ionic bonds and/or disulfide linkages.
| Protein | Polypeptide chains | Quaternary? |
|---|---|---|
| Haemoglobin | 4 | ✓ yes |
| Insulin | 2 | ✓ yes |
| Myoglobin | 1 | ✗ cannot have a quaternary structure |
- ① Transcription (nucleus): gene → mRNA
- ② Translation (ribosomes, free and on the rER): mRNA → polypeptide chain = primary structure
- ③ Post-translational modification / protein folding (rER) → secondary, tertiary, quaternary
Globular vs fibrous proteins
| Globular — soluble | Fibrous — insoluble | |
|---|---|---|
| R groups pointing outwards | hydrophilic ⇒ water soluble | hydrophobic ⇒ water insoluble |
| Shape | spherical / circular | long, narrow strands |
| pH & temperature | sensitive to changes | less sensitive |
| Examples | enzymes, haemoglobin | keratin, collagen |
Evidence: nails and hair (keratin) are never seen dissolving in water ⇒ fibrous proteins are insoluble. Enzymes are globular so are sensitive to pH & temperature.
Haemoglobin (globular)
- 1 Hb molecule = 4 polypeptide chains: 2 identical α-chains (α-globins) + 2 identical β-chains (β-globins) → quaternary structure.
- Each chain has a haem group (a prosthetic group) with iron (Fe²⁺) at its centre; Fe²⁺ reversibly binds one O₂ ⇒ 1 Hb holds 4 O₂.
Definition to learn: haemoglobin is an iron-containing protein.
Collagen (fibrous protein)
- Found in skin, tendons, cartilage, bones, teeth, walls of blood vessels; most common protein in animals; structural protein — up to 25 % of total protein of a mammalian body.
- High tensile strength (+ flexible); not easily affected by pH & temperature changes.
- Every 3rd amino acid is glycine (smallest) ⇒ the 3 chains can lie very close and form a tight coil (tropocollagen).
9. Water
70–95 % of cell mass; the human body is ~60–65 % water; ~90 % of blood plasma. Water is a polar molecule with a non-linear, bent shape. δ⁻ O attracts δ⁺ H of neighbours ⇒ hydrogen bonds between molecules.
① Excellent solvent for polar & ionic molecules
δ⁻ O surrounds Na⁺, δ⁺ H surrounds Cl⁻ ⇒ ions separate and dissolve. Water is therefore the transport medium in plants and animals (blood, xylem, phloem) and the medium of reactions in cytoplasm.
② High specific heat capacity
Definition: the amount of heat energy required to raise the temperature of one unit mass of water by 1 °C / 1 K. Q = m c ΔT ; c = Q / mΔT
To raise the temperature of a liquid, molecules must gain energy and move faster. H-bonds make it harder for molecules to move freely, so they must be broken ⇒ MORE heat energy is needed.
③ High latent heat of vaporisation
The heat energy needed to vaporise 1 g of liquid at constant temperature. The network of H-bonds means a high energy input is needed to change 1 g liquid water → vapour.
④ Cohesion & surface tension
Cohesion = attraction between molecules of the same kind. Surface tension = tendency of liquid surfaces at rest to shrink into the minimum surface area possible.
⑤ Adhesion
Attraction of water molecules for molecules of a different kind ⇒ water sticks to the sides of vessels.
⑥ Maximum density at 4 °C — anomalous behaviour
Normal liquid: heated → expands (volume ↑, density ↓); cooled → contracts (volume ↓, density ↑). Density = mass/volume, mass constant ⇒ d ∝ 1/V. Cooling water from 100 °C down to 4 °C: volume ↓, density ↑ (this part is normal contraction, not due to H-bonding). At 4 °C maximum density is reached; on cooling below 4 °C water expands (volume ↑, density ↓) ⇒ anomalous behaviour of water.
10. Quick Recap — Chapter Cheat-Sheet
- CHON = 4 main elements. Polymer = repeating monomers; all polymers are macromolecules, not all macromolecules are polymers (lipids!).
- Carbs: Cx(H₂O)y; mono → (CH₂O)ₓ; hexose C₆H₁₂O₆, pentose C₅H₁₀O₅, deoxyribose C₅H₁₀O₄.
- α-glucose: OH below on C1; β-glucose: OH above. Only difference.
- Maltose = α+α (α-1,4) · Sucrose = α-glucose + fructose · Lactose = glucose + galactose · Cellobiose = β+β (β-1,4, alternate unit flipped 180°).
- Glycosidic bond = covalent C–O–C, formed by condensation (–H₂O), broken by hydrolysis.
- Reducing sugars: all monosaccharides + maltose, lactose, cellobiose; sucrose is non-reducing; Benedict’s: blue → brick-red ppt (Cu²⁺ → Cu⁺). Non-reducing: boil with dilute HCl first, then Benedict’s.
- Polysaccharides: (n–1) H₂O lost; osmotically inactive, compact, insoluble, inert. Starch (amylose helix α-1,4; amylopectin branched α-1,4 + 1,6) · glycogen (more branched) · cellulose (β-glucose, 180° alternate, H-bonds → microfibrils → fibres).
- Resistance to digestion: amylose > amylopectin > glycogen.
- Lipids: triglyceride = glycerol + 3 fatty acids (3 ester bonds, –3 H₂O). Unsaturated (C=C) melt easily. Phospholipid = hydrophilic head + hydrophobic tails (amphipathic). Lipids give >2× energy per gram vs carbohydrates.
- Proteins: amino acid (–NH₂, –COOH, R, H; zwitterion). Peptide bond by condensation. 1° sequence (peptide) · 2° α-helix / β-sheet (H-bonds backbone) · 3° R-group bonds (H, hydrophobic, ionic, disulfide) · 4° ≥2 chains. Strength: hydrophobic < H-bond < ionic < covalent.
- Globular (soluble, spherical, hydrophilic R outside, e.g. Hb, enzymes) vs fibrous (insoluble, strands, hydrophobic R outside, e.g. keratin, collagen).
- Hb: 4 chains (2α + 2β), 4 haem groups with Fe²⁺, binds 4 O₂. Collagen: triple helix (every 3rd = glycine), covalent cross-links, high tensile strength.
- Water: polar, bent, H-bonds ⇒ solvent · high specific heat capacity · high latent heat of vaporisation (cooling) · cohesion / surface tension · adhesion (xylem) · max density at 4 °C (ice floats).