Year 12

AQA A level Biology Biological Molecules Notes

Biological Molecules

— Biology · AS Level (7402) · Chapter 2
★ Exam Tip: Chapter is full of drawing + identify marks — know the α / β glucose rings, the glycosidic bond in maltose / sucrose / cellobiose, condensation reactions, and compare starch · glycogen · cellulose in a table. Polysaccharide comparisons and amylose vs amylopectin come up in papers again and again.

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
Remember: carbs, proteins & lipids = the 3 macronutrients (needed in the diet in large amounts).

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.

“All polymers are macromolecules, but not all macromolecules are polymers”
polymer — same unit repeatsA B C A A A A A Bno repeat ⇒ NOT polymer= macromolecule onlyA B CA B CA B C 3 repeat units of ABC ⇒ polymer ✓
chain of identical units = polymer · irregular chain = macromolecule only
Why “non-sugars”? Polymers (polysaccharides) are tasteless / not sweet, so they are often called non-sugars. Water is not a macromolecule (simple H₂O). Carbs, proteins, nucleic acids = polymers; lipids = macromolecule only (explained in the lipids section).

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).

General formula of carbohydrates: Cx(H₂O)y

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):

CARBOHYDRATES Cx(H₂O)y Monosaccharides1 sugar unitDisaccharides2 sugar unitsPolysaccharidesmany sugar unitsgeneral formulaCₓH₂ₓOₓ = (CH₂O)ₓ① Hexoses (6 C)glucose, fructose,galactose C₆H₁₂O₆② Pentoses (5 C)ribose C₅H₁₀O₅deoxyribose C₅H₁₀O₄③ Trioses (3 C)sucrosemaltoselactosecellobiose• glycogen• starch• cellulose
syllabus: only hexoses & pentoses needed (trioses just exist)
Trick: number in the name = number of carbons: hexa-6, penta-5, tri-3 (hexagon has 6 sides!).
  • 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).

O HC1C2H OH C3HO H C4H OH C5H OH C6H OH CH₂OH
open chain — unstable
O12345 H OH H OH OH H H OH CH₂OH α-glucoseC1: OH BELOW
O12345 OH H H OH OH H H OH CH₂OH β-glucoseC1: OH ABOVE
The ONLY difference: position of the –OH on carbon 1
α → OH below the ring  |  β → OH above the ring
Trick: α starts with A ⇒ At the bottom (below); β starts with B ⇒ Boost up (above).

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).

Glycosidic bond = C – O – C link between 2 sugar molecules; it is a covalent bond
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
★ Most tested: maltose and sucrose (then lactose, cellobiose). Learn which monosaccharides make each one!
O12345 H OH H OH OH H H OH CH₂OH O12345 H OH H OH OH H H OH CH₂OH α-glucoseα-glucose OH HOcarbon 1 OH + carbon 4 OH react→ – H₂O
① two α-glucose lined up: OH on C1 (left) meets OH on C4 (right)
O12345 H OH H OH OH H H OH CH₂OH O12345 H OH H OH OH H H CH₂OH O α-1,4 glycosidic bondMALTOSE+ H₂O released
② H₂O lost; the leftover O links C1 and C4 ⇒ α-1,4 glycosidic bond (maltose)

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

OC₂C₅C₃C₄ CH₂OHCH₂OHOHOHOH straight chainCH₂OHC = OHO – C – HH – C – OHH – C – OHH – C – OHH“cottage-shaped”5-membered ringC1 & C6 both outside
fructose looks like a little cottage (house) — easy to identify in an MCQ
Syllabus: you are not asked to draw fructose or know its orientation — only to recognise it (cottage shape). Glucose: only C6 is outside the ring; fructose: C1 & C6 outside.

Fructose is a ketose (C=O in the middle, C2), a hexose like glucose and galactose.

Sucrose = α-glucose + fructose

OC₂C₅C₃C₄ CH₂OHCH₂OHOHOHOH O12345 H OH H OH OH H H OH CH₂OH OH HO– H₂Ofructose + α-glucose
① condensation: C1-OH of α-glucose + C2-OH of fructose
OC₂C₅C₃C₄ CH₂OHCH₂OHOHOHOH O12345 H H OH OH H H OH CH₂OH O glycosidic bondSUCROSE
② water lost, O bridges the rings = covalent glycosidic bond

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.

O12345 OH H H OH OH H H OH CH₂OH β-glucose O12345 OH H OH H H OH OH CH₂OH β-glucose (flipped 180°)C1 –OH upC4 –OH now up – H₂O
① right ring flipped by 180° so its C4–OH lines up with C1–OH of left ring
O12345 OH H H OH OH H H OH CH₂OH O12345 H OH H H OH CH₂OH O β-1,4 glycosidic bondCELLOBIOSE
② cellobiose: alternate unit is upside-down (β-1,4 link, C1 → C4)
Glycosidic bond (all of them): covalent bond between two sugar units, C–O–C, formed in a condensation reaction (–H₂O). Broken by hydrolysis (+H₂O).

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⁺).

Reducing sugar + Cu²⁺ (Benedict’s, blue) → oxidised sugar + Cu⁺ (red-brown ppt)

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.

blue0 g% green0.5–1 g% yellow1–1.5 g% orange1.5–2 g% brick red>2 g% more reducing sugar →
Benedict’s colour scale: blue → green → yellow → orange-red → brick-red
Why does sucrose fail? Its reducing groups of both monosaccharides are used up in the glycosidic bond (C1 glucose – C2 fructose).

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.

sucrosehydrolysisdilute HClglucose +fructosenon-reducingreducing sugars ✓
sucrose → 2 monosaccharides after acid hydrolysis

6. Polysaccharides

Made by joining many monosaccharide molecules (monomers) by condensation. Examples: starch, glycogen, cellulose — all non-reducing and osmotically inactive.

n C₆H₁₂O₆ → (C₆H₁₀O₅)ₙ + (n − 1) H₂O

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:

Storage polysaccharide is: compact · inert (unreactive) · insoluble ⇒ osmotically inactive. Plants → starch; animals (and fungi) → glycogen. When needed, glucose is quickly made available again by enzyme-controlled hydrolysis.
↑ solute conc.WP ↓(glucose) H₂O in byosmosis
free glucose = osmotically active → water drawn into the cell

Starch (made of α-glucose) — amylose + amylopectin

enzyme endenzyme endhelical · α-1,4unbranched α-1,6branch pointα-1,4 in chainsbranched · non-helicalα-1,4 and α-1,6AMYLOSEAMYLOPECTIN
amylose = coiled helix, unbranched; amylopectin = branched (red dots = α-1,6 branch points)
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
Frequently asked: which of amylose / amylopectin is more resistant to digestion? → amylose (unbranched, helical, only 2 ends for enzymes). Amylopectin: enzymes can attack at the ends and the many branch ends ⇒ digested faster.

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
Resistance to digestion (hydrolysis):
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).

dot = CH₂OH: up, down, up, down … (alternate units flipped 180°)① β-glucose monomer② cellulose molecule (β-1,4) H-bonds③ microfibril: 60–70 cellulose molecules held by H-bonds④ many microfibrils (H-bonds) ⇒ cellulose FIBRE⇒ high tensile strength
cellulose: chain → microfibril → fibre
Key link: straight β-chains lie side-by-side, many H-bonds hold them together — individually weak but together very strong = high tensile strength (that is why cell walls resist stretching/bursting).

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 ✗ ✗ ✗ ✗
Note on H-bonds: the board table ticks hydrogen bonds for all four. In class: H-bonding between molecules is the very important feature of cellulose (chains bundle into microfibrils); in starch & glycogen the chains are helical/branched so they do not pack together this way.

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).

Glyceride = an ester formed by a fatty acid combining with glycerol (alcohol)
H–C–OHHO–C OH–C–OHHO–C OH–C–OHHO–C O glycerol3 fatty acids – 3 H₂OH–C–O –CO H–C–O –CO H–C–O –CO TRIGLYCERIDE3 ester bonds (–COO–)
3 –OH of glycerol + 3 –COOH of fatty acids → 3 ester bonds + 3 H₂O (condensation / esterification)

Fatty acids: saturated vs unsaturated

COOHsaturated: only C–Cclosely packed ⇒ solid at r.t.p. (fat)do NOT melt easily COOHunsaturated: has C = C (kink)loose packing ⇒ liquid at r.t.p. (oil)MELT EASILY
a C=C double bond bends the chain so molecules cannot pack closely
  • 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.

Pglycerolphosphate headhydrophilic · soluble (polar)lipid / fatty acid tailshydrophobic · insoluble(non-polar)
phospholipid: polar head + 2 non-polar tails

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.
Why are lipids not polymers? They are not built from repeating units of the same monomer, so they stay “just a macromolecule”.

8. Proteins (made of amino acids)

Structure of an amino acid (building block)

R H₂N C C O OH Hamine / aminogroupcarboxylic acidgroupR varies forevery amino acid
central C: –NH₂ , –COOH , –H and R group
R H₃N+ C C O O–zwitterion(electrically neutral)+ charge– charge
zwitterion: –NH₃⁺ and –COO⁻ ⇒ overall neutral
R groups to remember: only glycine (R = H, smallest amino acid) and cysteine (R contains –SH, forms disulfide bonds).

Peptide bond (condensation)

–COOH of one amino acid + –NH₂ of the next → –H₂O → peptide bond (–CO–NH–). 2 amino acids = dipeptide; many = polypeptide.

H₂N–CHR–C–OOH+H–N–CHR–COOH↓ – H₂OH₂N–CHR–C–N–CHR–COOHOH peptide bonddipeptide
condensation: OH from acid + H from amine leave as H₂O
AAAA———①②③4 amino acids ⇒ 3 peptide bonds
n amino acids joined by (n – 1) peptide bonds

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.

α-helixhelical β-pleated sheetribbon / arrow shaped
secondary structure (H-bonds between C=O and N–H of the backbone)
Why H-bonds? O, F, N are highly electronegative ⇒ C=O (δ⁻) and N–H (δ⁺) attract. Primary & secondary use the backbone (peptide bonds / H-bonds); tertiary & quaternary use R groups.

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.

amino acidamino acidPPhydrogen bonds amino acidamino acidNPNPhydrophobic interactions amino acidamino acid+–ionic bondingcysteineCH₂–S–HH–S–H₂Ccysteine↓ 2H lostcysteineCH₂–S–S–H₂Ccysteinedisulfide linkage (covalent)
the 4 types of tertiary-structure bonding between R groups
Bond strength (weakest → strongest):
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.

tertiary1 polypeptide chainquaternary (2 subunits)→ 2 chains associate →
tertiary = one chain; quaternary = ≥ 2 chains together
Protein Polypeptide chains Quaternary?
Haemoglobin 4 ✓ yes
Insulin 2 ✓ yes
Myoglobin 1 ✗ cannot have a quaternary structure
Rule: 2 or more polypeptide chains (same or different) ⇒ quaternary structure. A single-chain protein can never have one.
Recall & reconnect — protein synthesis
  • 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)

α-chainβ-chainβ-chainα-chain ● haem groupwith Fe²⁺ at centre1 Hb + 4 O₂ → HbO₈oxyhaemoglobin
quaternary structure of haemoglobin: 4 chains, each with a haem
  • 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.
Hb + 4 O₂ ⇌ HbO₈  (oxyhaemoglobin)

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).
associate via H-bonds ⇒ 3 helical polypeptide chainsTROPOCOLLAGENtriple helix = collagen molecule
3 helical chains → H-bonds → tight rope-like tropocollagen
covalent cross-links② many tropocollagen molecules –(covalent cross-links)→ collagen FIBRIL③ many collagen fibrils → COLLAGEN FIBRE① 3 helical chains –(H-bonds)→ tropocollagen
collagen build-up: chains → tropocollagen → fibrils → fibre
Summary: Collagen is the main structural protein of animals. The fundamental unit of the fibre = 3 helical polypeptide chains wound around each other forming a triple helix (tropocollagen) with high tensile strength.

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.

δ⁻O H δ⁺H δ⁺δ⁻O H δ⁺H δ⁺ hydrogen bond
bent, polar molecule; H-bonds between neighbouring 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.

Cl⁻Na⁺H(δ⁺)δ⁻Oδ⁻O ··· Na⁺Cl⁻···H
water molecules orient around ions (hydration shell)

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.

Advantage — stable temperature: (i) human body temperature stays within a narrow range ⇒ optimum enzyme activity not hindered (enzymes are globular proteins sensitive to temperature); (ii) large water bodies keep a narrow temperature range ⇒ stable habitat for aquatic life.

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.

Advantage — cooling effect: lets the body remove a large amount of heat with minimum loss of water (as sweat).

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.

airbulk molecules pulled from all directionssurface molecules pulled inward
surface molecules are pulled inward ⇒ they occupy minimum surface area ⇒ habitat for light organisms (e.g. pond skater, mosquito)

⑤ Adhesion

Attraction of water molecules for molecules of a different kind ⇒ water sticks to the sides of vessels.

Link: cohesion & adhesion are both essential for the movement of water up the xylem vessels in plants.

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.

densitytemp / °Cmax. density at 4 °C04100cooling: vol ↓, density ↑← below 4 °C: expands
density rises on cooling until 4 °C, then falls — ice is less dense than water
ICE: H-bonds stableopen lattice ⇒ more space LIQUID water: H-bondsconstantly break & re-form
ice = expanded lattice (more space occupied by ice molecules); liquid = closer packed
Why it matters: ice floats on top of ponds/lakes, insulating the water below ⇒ aquatic life survives (stable habitat).

10. Quick Recap — Chapter Cheat-Sheet

✓ Quick Recap
  • 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).