G10 Biology · Chemistry of Life

G10 Biology Study Guide

6 Lessons: Chemistry of Life, Macromolecules, Proteins & Enzymes

The Chemistry of Life

1.1 Atoms, Elements & Matter

Life is built from four key elements: Carbon (C), Hydrogen (H), Oxygen (O), and Nitrogen (N). Understanding atomic bonding is foundational to biology.

TermDefinitionExample
ElementCannot be broken down into simpler substancesCarbon, Oxygen
AtomSmallest unit of an elementA single carbon atom
MoleculeTwo or more atoms joined by chemical bondsH₂O (water)
Covalent BondSharing electrons between atomsC–H bond in glucose
Ionic BondTransfer of electrons; opposite charges attractNaCl (salt)
Valence ShellOutermost electron shell; atoms bond to fill itCarbon has 4 valence e⁻

Carbon: The Backbone of Life

Carbon has 4 valence electrons → forms 4 covalent bonds. This versatility makes carbon the foundation of all organic molecules. Organic = containing C found in living systems. Exception: CO₂ and carbonates are inorganic.

1.2 Organic vs Inorganic
PropertyOrganicInorganic
DefinitionContains carbon, found in living systemsDoes not contain C–H bonds
ExamplesGlucose, proteins, DNA, lipidsCO₂, H₂O, NaCl

💡Key Exception

CO₂ contains carbon but is INORGANIC because it lacks C–H bonds.

1.3 Protein Powder Phenomenon

Protein powder is a popular supplement. The key question: How do the chemicals in protein powder help absorb proteins? Enzymes in the digestive system break peptide bonds via hydrolysis, releasing amino acids for absorption in the intestine.

Building Biomolecules

2.1 Four Main Biomolecules

Life depends on four classes of macromolecules. All contain carbon and are built from smaller subunits (monomers).

Hydrogen (H)
Carbon (C)
Oxygen (O)
Nitrogen (N)
BiomoleculeElementsMonomerPolymerShape
CarbohydratesC, H, O (1:2:1)MonosaccharidePolysaccharideRing (hexagon)
LipidsC, H, O (much more C & H)Glycerol + Fatty AcidsNot a true polymerLong chain
ProteinsC, H, O, N (some S)Amino AcidPolypeptideCentral C + NH₂ + COOH + R
Nucleic AcidsC, H, O, N, PNucleotideDNA / RNAChain of nucleotides
2.2 Identifying Macromolecules

📊Element Mnemonic: CHO / CHON / CHONP

Carbs & Lipids = CHO
Proteins = CHON
Nucleic Acids = CHONP

⚠️Watch Out: Carbs vs Lipids

Both contain only CHO! Lipids have MUCH MORE C and H relative to O and form long chains. Carbs have a 1:2:1 ratio.

Metabolism & Macromolecules

3.1 Monomer vs Polymer
ConceptDefinitionAnalogy
MonomerA single building block unit1 Lego block
PolymerA chain of many monomersLego building
PolymerizationProcess of linking monomers into polymersSnapping Legos together
3.2 Condensation vs Hydrolysis
ReactionWhat HappensWaterMetabolism
CondensationMonomers join → polymerRELEASEDAnabolism (合成代谢)
HydrolysisPolymer → monomersUSEDCatabolism (分解代谢)
Monomer A
+
Monomer B
↓ Condensation: H₂O released ↓
Dimer (A–B)
↓ Hydrolysis: H₂O added ↓
Monomer A
+
Monomer B

📊Metabolism Definitions

Metabolism = all enzyme-catalyzed reactions in a cell
Anabolism = building complex molecules (condensation)
Catabolism = breaking complex molecules (hydrolysis)

3.3 Detailed Functions
MacromoleculeKey FunctionsExamplesBuild / Break
CarbohydratesFast energy, structural support, storageGlucose, starch, glycogen, celluloseCondensation / Hydrolysis
LipidsLong-term energy, membrane, insulation, hormonesOil, butter, wax, cholesterolN/A
ProteinsStructure, transport, enzymes, antibodiesCollagen, hemoglobin, insulinCondensation / Hydrolysis
Nucleic AcidsStore & transmit genetic infoDNA, RNACondensation / Hydrolysis

Protein Structure & Function

4.1 Amino Acids & Peptide Bonds

20 different amino acids exist in nature. Each has three parts:

NH₂
Amino group
C
COOH
Carboxyl group
H
R group
(unique per amino acid)

Amino acids link via PEPTIDE BONDS (covalent) through condensation. Chain = POLYPEPTIDE. Sequence (coded by DNA) determines 3D structure → function.

4.2 Four Levels of Protein Structure
LevelNameDescriptionBond
1PrimarySequence of amino acidsPeptide bonds
2SecondaryFolding (α-helix, β-sheet)Hydrogen bonds
3Tertiary3D arrangementH-bonds, disulfide, ionic
4QuaternaryMultiple polypeptidesSame as tertiary
4.3 Fibrous vs Globular Proteins
FeatureFibrousGlobular
ShapeLong strandsRounded
RoleStructural supportFunctional (transport, catalytic)
SolubilityLess solubleMore soluble
ExamplesCollagen, Keratin, ActinHemoglobin, Insulin, Enzymes
4.4 Denaturation & Proteome

Denaturation = Irreversible!

Caused by extreme pH or high temperature. Destroys secondary, tertiary, quaternary structure. Primary structure (amino acid sequence) remains intact.

Example Proteins

ProteinStructureFunction
Insulin2 chains (21 + 30 AA)Hormone; regulates blood sugar
CollagenTriple helixSkin, tendon, bone support
Hemoglobin4 subunitsTransports O₂ in blood

📊Proteome vs Genome

Genome = complete set of genes
Proteome = complete set of proteins
Every individual has a UNIQUE proteome.

Enzymes

5.1 Enzyme Properties & Specificity

Enzymes are LARGE GLOBULAR PROTEINS acting as organic catalysts. They lower activation energy, increase reaction rates, are NOT consumed, and work at low concentrations.

Key TermDefinition
EnzymeGlobular protein catalyst
Active SiteRegion where substrate binds
SubstrateMolecule the enzyme acts on
Activation EnergyMinimum energy to start a reaction
SaturationAll active sites occupied

Two Models of Enzyme Specificity

The active site fits the substrate perfectly like a key in a lock. The active site is a rigid, exact shape.

The active site changes shape slightly when substrate binds — like a glove fitting around a hand. This is the MORE ACCURATE model.

Phenomenon: Lactose Intolerance

Lactose (milk sugar) is broken by LACTASE into glucose + galactose. Insufficient lactase → undigested lactose → bacteria produce CO₂, H₂, methane → bloating. Lactose intolerance is the NATURAL state for most mammals.

5.2 Factors Affecting Enzyme Activity

Effect of Temperature

Temperature vs Enzyme Activity / 温度 vs 酶活性 Activity / 活性 Temperature (°C) / 温度 020406080100 Optimal ~37°C Denaturation! / 变性!

Effect of pH

pH vs Enzyme Activity / pH vs 酶活性 Activity / 活性 pH 02468101214 Optimal pH / 最佳pH

Effect of Substrate Concentration

Substrate Concentration vs Rate / 底物浓度 vs 反应速率 Rate / 速率 Substrate Conc. / 底物浓度 Vmax ← All active sites busy → / ← 所有活性位点已满 →

💡Key Insight

At saturation, increasing substrate has NO EFFECT. To go faster, you need more enzyme.

5.3 Enzyme Denaturation

How Enzymes Denature

High temperature: Extra kinetic energy → vibration → breaks bonds → active site changes
Extreme pH: Breaks hydrogen bonds → active site changes
Result: Substrate CANNOT bind → enzyme stops. IRREVERSIBLE.

Master Comparison Table

CarbsLipidsProteinsNucleic Acids
ElementsC, H, OC, H, OC, H, O, N (S)C, H, O, N, P
MonomerMonosaccharideGlycerol + Fatty AcidsAmino AcidNucleotide
PolymerPolysaccharideNot a true polymerPolypeptideDNA / RNA
Energy RoleFAST energyLONG-TERM storageStructural, transportGenetic info
ExamplesGlucose, starch, glycogenButter, oil, wax, cholesterolCollagen, hemoglobin, insulinDNA, RNA
BuildCondensationN/ACondensationCondensation
BreakHydrolysisN/AHydrolysisHydrolysis

Key Definitions Glossary

TermDefinitionTermDefinition
MatterHas mass and takes up spaceAnabolismBuilding up molecules
ElementCannot be broken down furtherCatabolismBreaking down molecules
Covalent BondSharing electronsDenaturationLoss of 3D structure (irreversible)
MonomerSingle building blockProteomeComplete set of proteins
PolymerChain of many monomersActive SiteRegion where substrate binds
CondensationMonomers join; H₂O releasedEnzymeGlobular protein catalyst
HydrolysisPolymer broken; H₂O usedLactaseBreaks lactose → glucose + galactose

G10 Biology Quiz

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