IB CHEMISTRY

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PAST PAPER QS ARE AT THE BOTTOM
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STOICHIOMETRIC RELATIONSHIPS 2

ATOMIC STRUCTURE 2

PERIODICITY 2

BONDING 2

ENERGETICS 4
Definition compendium (oh boy i hate definitions) 5

EQUILIBRIUM 5

ACIDS AND BASES 6

SL 6
HL 7

REDOX 8
SL 8
HL 8

ORGANIC CHEMISTRY 9
Some wanker’s haphazardly drawn chart: 10

ANALYTICAL CHEMISTRY 11

OPTION B: BIOCHEMISTRY 11
b.1 introduction to biochemistry 11
b.2 proteins and enzymes 12
proteins and heredity 12
2-amino acids and peptides 12
Essential 2-amino acids 12
2-amino acids as zwitterions 12
Acid-base properties of 2-amino acids and buffers 13
Gel electrophoresis 13
Paper chromatography 14
intermolecular forces in amino acids 14
Peptides 15
B.3 lipids 16
 Iodine number 17
Rancidity of fats 17
Health 17
Calculating energy content 17
Phospholipids 17
B.5 Vitamins 18

OPTION C: ENERGY 19
C.1 - Energy sources 19
C.2 - Fossil fuels 19
C.3 - Nuclear fusion and fission 20
C.4 - Solar energy 21

PAST PAPER QUESTIONS 22

Periodicity 22
Bonding 22
Equilibrium 22
Acids and bases 23
Organic chemistry 23
Nature of science 24

STOICHIOMETRIC RELATIONSHIPS 
https://docs.google.com/document/d/11h5VsJd_IB7ThAVM3SA2VHE5iNbsEOob2M85uyvg
OeU/edit

ATOMIC STRUCTURE 
https://docs.google.com/document/d/1VW09SGxNXNZjw-htP2RvCoC912RLB4GMA8rlLv7t
M6c/edit?usp=sharing

PERIODICITY 
https://docs.google.com/document/d/1xTEQEmCbPuSH_Q502oNfgwGcsP0b7keJwB8vXBm
zcaw/edit?usp=sharing

BONDING 
https://docs.google.com/document/d/1-uSTmiSRc3iW9abcUv5CX4OlyRyx8swH2WTFQQFz
LNw/edit?usp=sharing

● Ionic compounds usually have lattice structures

● Single atom - ide; polyatomic - ite, ate
● Ionic compounds have higher boiling points and are less volatile
● Ionic compounds are soluble in water
● Covalent compounds do not conduct electricity
● Covalent compounds are soluble in solutions which form H-bonds
 ● As bonding increases (single, double, triple), the bond length decreases and bond
strength increases
● electronegativity difference > 1.7, then ionic bond
● 0.4 < e-vity diff < 1.7, then polar covalent bond
● e-vity diff < 0.4, then non-polar covalent bond
● partial charge: ​δ− or δ+

Coordination number: number of ligands

Compound shapes predicted by VSEPR (SL):

# of electron bonded lone pairs molecular angles examples

electron domain pairs geometry
domains geometry

2 linear 2 0 linear 180 BrCl​2

3 planar 3 0 planar 120 BF​3

trigonal trigonal

4 tetrahedral 4 0 tetrahedral 109.5 CH​4

4 “ 3 1 trigonal 107.3 NH​3

pyramidal

4 “ 2 2 bent 104.5 H​2​O

Compound shapes predicted by VSEPR (HL):

# of electron bond lone molecular angles examples

electron domain pairs pairs geometry
s geometry
 5 trigonal 5 0 trigonal 90, 120 PCL​5
bipyramidal bipyramidal

5 “ 4 1 seesaw 90, < 120 SCl​4

5 “ 3 2 T-shaped 90 ICl​3

5 “ 2 3 linear 180 I​3​-

6 octahedral 6 0 octahedral 90, 90 SF​4

6 “ 5 1 square pyramidal 90, 90 BrF​3

6 “ 4 2 square planar 90 XeF​4

Structure of benzene:

Structure of ozone:

Hybridization:
● single bond: sp​3​, tetrahedral
● double bond: sp​2​, trigonal planar
● triple bond: sp, linear

Formal charge:
● formula: number of valence electrons - 0.5 shared electrons - lone electrons

ENERGETICS 
● energy change when bonds are broken is known as enthalpy change (​△H)
● heat is a form of energy, temperature is a measure of kinetic energy
● when △H = -ve, energy is released
● when △H = +ve, energy is absorbed
 ● Calorimetry: q = mc△T
○ standard state: at 100 kpa and 298 K
○ limitations: assumed specific heat capacity of water, loss of heat
● Hess’ law: the energy change will be the same regardless of the path taken
● enthalpy of combustion: heat change from combustion of 1 mole of a substance in
excess oxygen under standard states
● △H​0​ formation = sum of △H products - sum of △H reactants
● △H​0​ combustion = sum of △H reactants - sum of △H products
● Assumption: intermolecular forces do not influence enthalpy

Born-Haber cycle:

Definition compendium (oh boy i hate definitions) 

● Enthalpy of Atomization: ​The energy required to form ​one mole​ of individual ​gaseous
atoms of an element, from the ​element in its standard state.
● Electron affinity: ​The enthalpy associated with one mole of gaseous atoms or anions gaining
an electron.
● Ionization energy: The enthalpy associated with​ one mole of a gaseous element on
cation to lose one mole of to form one mole of gaseous cations
● Lattice enthalpy: ​The ​∆​H associated with converting one mole of a solid ionic compound
into individual gaseous anions and cations
● Enthalpy of solution: ​The change in heat associated with dissolving one mole of a solid
ionic compound in an infinite amount of water
● Enthalpy of hydration: The change in heat when one mole of gaseous ions dissolve
in an infinite amount of water.
● Standard enthalpy of formation: ​The enthalpy change associated with forming​ 1 mol​ of a
substance from its element in their standard states
● Standard enthalpy of combustion: ​The amount of energy released when ​1 mol​ of a
substance is completely combusted with excess O2
 EQUILIBRIUM 

ACIDS AND BASES 

SL 
● Bronsted-Lowry acid: H​+​/H​3​O​+ ​donor
● Bronsted-Lowry base: H​+​/H​3​O​+​ acceptor
● Amphiprotic species can both donate and accept a proton
○ eg: H20, HCO3-, HSO4-
● All amphiprotic species are amphoteric, but not all amphoteric species are
amphiprotic
● Amphoteric species eg: Al2O3, ZnO
● An acid and its conjugate base differ by one proton (acid loses proton)
● A base and its conjugate acid differ by one proton (base gains proton)
● Metal oxides are basic, non-metal oxides are acidic

REACTIONS OF ACIDS:

1. acid + active metal -> H​2​ + salt

a. 2HCl + Zn -> H2 + ZnCl2
2. acid + carbonate -> salt + CO2 + H2O
a. 2HCl + Na2CO3 -> 2NaCl + CO2 + H2O
3. acid + hydrogencarbonate -> salt + CO2 + H2O
a. HCl + NaHCO3 -> NaCl + CO2 +H2O

● pH = -log​10​[H+]
● [H+] = 10​-pH
● Kw = [H+][OH-]
○ if [H+] = [OH-], pH= 7
○ if [H+] > [OH-], pH< 7
○ if [H+] < [OH-], pH> 7

Strong acid Weak acid

completely ionizes partially ionizes

forms weak conjugate base forms strong conjugate base

high electrical conduction low electrical conduction

vigorous reactions with active metals slow reactions with active metals
 ● acid deposition has a pH of less than 5.0
● source of SO2: burning fossil fuels, volcanoes
● source of NO2: vehicles, lightning

1. carbonic acid
a. C + O2 -> CO2
b. CO2 + H2O -> H2CO3
c. H2CO3 ​⇌ H+ + HCO3-
2. nitric acid
a. N2 + O2 -> 2NO
b. NO + O2 -> NO2
c. NO2 + H2O -> HNO2 + HNO3
d. 4NO2 + O2 + H2O -> 4HNO3
3. sulfuric acid
a. S + O2 -> SO2
b. SO2 +H2O -> H2SO4
c. 2SO2 + O2 -> 2SO3
d. SO3 + H2O -> H2SO4

Pre-combustion methods for SO2 removal:

1. hydrosulfurization: catalyst removes sulfur from natural gas and refined petroleum
2. metal sulfides can be removed by crushing and washing
3. fluidized bed combustion: coal mixed with limestone during combustion

HL 
● The salt of a weak acid is a basic in nature
● The salt of a weak base is acidic in nature
○ CH3COO- + H+ ​⇌ CH3COOH + OH-
■ CH3COONa is a basic salt
○ NH4+ + H2O ⇌ NH3 + H3O+
■ NH4Cl is an acidic salt
● [Fe(H2O)6]3+ is acidic, as one of the H2O coordinate bond becomes long, releasing
H+ and leaving OH- as a ligand
○ [Fe(H2O)6]3+ -> [Fe(H2O)5(OH-)]2+ + H+

● Lewis acid: accepts a pair of electrons

● Lewis base: donates a pair of electrons
● When a Lewis base donates a pair of electrons to a Lewis acids, a coordinate bond is
formed
● A nucleophile is a Lewis base; it either can donate a pair of electrons or is negatively
charged
● An electrophile is a Lewis acid; it either accepts a pair of electrons or is positively
charged
 ● Electrophiles have incomplete octets
● Transition metal ions in solution are Lewis acids
● Ligands are Lewis acids

● Ka x Kb = Kw = 1 x 10​-14​ at 298 K
● pKa + pKb = pKw = 14 at 298 K

REDOX 

SL 
● oxidation: gain of O, loss of H, loss of e-
● reduction: gain of H, loss of O, gain of e-
● oxidizing agents are themselves reduced
● reducing agents are themselves oxidized
● activity series is based on element’s strength as reducing agents
● redox titration: used to determine the concentration of a solution using an oxidizing or
reducing agent

Winkler’s method: used to determine the amount of dissolved O2 in water

1. 2Mn2 + 4OH- + O2 -> 2MnO2 + 2H2O
2. MnO2 + 4H+ + 2I- -> I2 + Mn2+ + 2H2O
3. I2 + 2S2O3 -> S4O6/2- + 2I-

Electromotive Force (EMF): E​0​ red - E​0​ ox

● Voltaic cells convert chemical energy to electrical energy

● Electrolytic cells produce electricity from chemical reactions
● In voltaic cells, oxidation occurs at the anode which is the negative electrode
● In electrolytic cells, oxidation occurs at the anode which is the positive electrode
● Cell diagram convention:
○ Zn | Zn​2+​(0.1 M)​ || Cu​2+​(0.1 M)​ | Cu
○ anode first then cathode

HL 
Standard Hydrogen Electrode (SHE)
1. 1 M (mol/dm3) concentration (aq)
2. 298 K
3. 1 atm / 10​5​ Pa
4. Platinum electrode
5. H2 gas
Photochromatic glasses:
● AgCl + CuCl ​⇌ Ag + Cu2+
● forward reaction makes the glasses black-coloured
● backward reaction makes the glasses transparent

△G​0​ = -nFE​0
● when E = -ve, △G = +ve (non-spontaneous)
● when E = +ve, △G = -ve (spontaneous)
ORGANIC CHEMISTRY 

Reactants Products Reagent/condition Mechanism

Alkene + Alkane
Hydrogen

Primary alcohol Aldehyde Acidified Oxidation

potassium (IV)
dichromate
(orange to green)
Distillation

Primary alcohol Carboxylic acid Acidified Oxidation

potassium (IV)
dichromate
(orange to green)
Reflux

Secondary alcohol Ketone Acidified Oxidation

potassium (IV)
dichromate
(orange to green)
 
Some wanker’s haphazardly drawn chart: 
 ANALYTICAL CHEMISTRY 

● ​Index
of hydrogen deficiency
○ AKA degree of unsaturation
○ How many more H2s can fit onto the molecule
○ IHD = ( 2*(# of carbons) + 2 - (# of hydrogens) ) / 2
○ Count halogens as hydrogens
○ Ignore O & S
○ Add 1 C and 1 H for each nitrogen present
○ alternate equation: (2C + 2 - H - X + N)/2
■ where C= carbon, H= hydrogen, X= halogen, N= nitrogen
● HNMR
○ Detects proton spins with magnetic field
○ Measures a variety of things
■ The number of general peaks signify the number of different hydrogen
environments
● The smaller subpeaks signify the number of hydrogens in
adjacent carbons + 1 (man this is hard to explain)
■ The location of the peaks signify certain groups
● IR spectrometry
○ The dips show the bonds that are present in the molecule
● Mass spectrometry
○ Mass / charge
○ Take note of only the significant peaks
○ The difference between each of the peaks can be indicative of certain sliced
parts of the molecule

OPTION B: BIOCHEMISTRY 
(yay)
i can write up a doc for this when i study it later today (from the study guide, not the whole
textbook) THANK YOUUUU - i’ll start it right now

b.1 introduction to biochemistry

● Studies the chemical processes in living cells at a molecular level
● Metabolism = biochemical processes
● Anabolic​ reactions: simple organic/inorganic molecules → large molecules, reducing
entropy. Cannot be spontaneous, which is supplied by catabolic reactions or photosynthesis
● Catabolic​ reactions: complex molecules are broken into smaller fragments

Water
● Nearly all biopolymers form by condensation reactions that release water as a by-product
● Glucose is polycondensed in plants to produce amylose (a component of starch)
● Amylose is hydrolysed into glucose
b.2 proteins and enzymes 
● Proteins are polymers of 2-amino acids
● Amino acids are joined by amide links/peptide bonds
● Amino acids are amphoteric
● Amino acids can exist as zwitterions, cations, and anions
● Enzyme activity is sensitive to changes in:
○ Temperature
○ pH
○ heavy metal ions

proteins and heredity 

● in 19​th​ century, people used to think that genetic information was stored in proteins
● it was revealed that nucleic acids instead were the true carriers of genetic information

2-amino acids and peptides 

● simple proteins are linear polymers of 2-amino acids
● proteins are joined together by amide links/peptide bonds
● peptides​: shorter polymers, less than 20 residues of 2-amino acids
● polypeptides​: longer peptides or small proteins, 20-50 structural units
● proteins​: more than 50 structural units
● peptides, polypeptides, and proteins are polycondensation polyers of 2-amino acids
● there are more than 500 naturally occurring amino acids
● only 20 amino acids are proteinogenic
○ used by living organisms as building blocks of proteins
● all of these amino acids have an amino and carboxyl group attached to the c-2 carbon, hence
2-amino acids
● 2-amino acids = proteinogenic amino acids

Essential 2-amino acids 

● Amino acids that must be supplied in the diet because they aren’t synthesised in the human
body are ​essential
● Non-essential amino acids can become essential under certain circumstances

2-amino acids as zwitterions 

● 2-aminoacids are amphoteric
● COOH is weakly acidic and NH2 is weakly basic
● In neutral aqueous solutions, both functional groups are completely ionised
● The ​migration​ of a ​proton​ from the COOH group to the NH group is an ​intramolecular
neutralisation reaction​ that creates a ​zwitterion
● ·​A zwitterion has net zero charge
● The NH3+ group in a zwitterion is the ​acidic centre​, which can ​lose a proton​ in strong
alkaline​ solutions to produce the ​anionic​ form of the amino acid
● The COO- group is the basic centre that can be protonated in strong acidic solutions to
create the ​cationic ​form of the amino acid
 ●
● The pH where the net charge is 0 is the ​isoelectric point (pI)
○ Each amino acid has a specific pI value
● Additional carboxyl group lowers the pI, additional amine group increases the pI
● pH < pI
○ add H+ → cationic form increases, zwitterion form decreases
● pH > pI
○ add OH- → anionic form increases, zwitterion form decreases
● zwitterions always remain the most abundant species unless it’s very acidic/alkaline

Acid-base properties of 2-amino acids and buffers 

● Pairs differing by a single proton (H+) are conjugate acid-base pair
[conjugate base] [H + ]
● Ka = [conjugate acid]
● Cationic forms of 2-amino acids with non-ionisable side-chains have two acidic centres,
-COOH and -NH3, and so there are two dissociation constants
○ Carboxyl group has relatively high acidity and dissociates more easily than the
protonated amino group
● Only two of the three forms (cation, zwitterion, anion) can be present at the same time and
one of them is always the zwitterion
● A strong acid is neutralised by the conjugate base of the buffer
● A strong base reacts with the conjugate acid
● Zwitterion + H+ ​→​cation
● Anion + H+ ​→​zwitterion
● Cation + OH- ​→​zwitterion + H2O
● Zwitterion + OH- ​→​anion + H2O
● At pH = pKa1 and pH = pKa2, the amino acid reaches its maximum buffer capacity and can
neutralise the greatest amount of strong acid or base

Gel electrophoresis 
● a mixture of amino acids is placed in the centre of a square plate
● the square plate is covered with agarose or polyacrylamide gel
● the gel is saturated with a buffer solution to maintain a constant pH
● depending on the pH of the buffer solution, the amino acids in the mixture will have various
charges
● two electrodes are connected to the opposite sides of the gel and there is an electric current
● negatively charged amino acids move to the positively charged electrode (anode)
● distance travelled is dependent on pI
 ● once separation is complete, ninhydrin (a locating agent) forms coloured compounds with
the amino acids
● if separation is incomplete, the plate can be rotated 90 degrees and electrophoresis can be
completed at a different pH
○ amino acids will move perpendicular to their original direction, separating
overlapping spots
● isoelectric focusing ​→​concentrating proteins in certain areas of the gel
● protein moves in the electric field until pH = pI
○ 0 net charge ​→​immobile

Paper chromatography 
● spot of liquid samples containing unknown amino acids is placed at the start line
● known amino acids are also placed at the start line
● stationary phase​: chromatographic paper
● mobile phase/eluent​: the solvent
● solvent rises up by capillary action
● more soluble: spend more time in the mobile phase, move up faster
● ninhydrin (locating agent) make the spots visible
● retention factor: ratio of the distances travelled by each spot to the distance travelled by the
solvent front
● solvent front is at the top
● each amino acid has a specific Rf
● chromatographic paper is made up of cellulose (a polysaccharide) that absorbs polar
compounds
● solvent has to be polar. If not, the amino acids will stay at the start line
● most common solvents: moderately polar alcohols, esters, chlorinated hydrocarbons (but
not anymore because of environment)
● turn 90 degrees if they’re overlapping
● thin-layer chromatography
○ adsorbent (silica, alumina, or cellulose) is placed on a flat plate (aluminium foil or
glass)
○ faster and more efficient separation
○ wide choice of stationary phases
● column chromatography
○ allows isolation of individual compounds
○ determines the quantitative composition of the mixture
● water is too polar so the amino acids may just all go to the solvent end point

intermolecular forces in amino acids 

● as a solid, amino acids are zwitterions held together by strong ionic forces between the two
functional groups
● all proteinogenic amino acids are/have:
○ crystalline solids
○ high melting points
 ○ readily soluble in water → ionic forces are placed by ion-dipole interactions and
hydrogen bonds between zwitterions and polar water
○ insoluble in non-polar organic solvents ​→​can oly form van der Walls’ forces, too
weak for overcoming lattice energy of ionic solids

Peptides 
● Terminal NH3 and COOH groups can be ionised to produce polyions
● Have pI
● Act as acid-base buffers
● Maintain a constant pH of biological fluids
● Perform regulatory and signalling functions
● E.g. growth hormones, regulating cell reproduction and tissue regeneration
● E.g. endorphins, inhibiting transmission of pain signals
● E.g. glutathione (tripeptide), a natural antioxidant
● Easily digestible
● Can be used as a source of 2-amino acids for the biosynthesis of proteins
● Native states/structures​: properly folded, contains all subunits
● Denatured​: do not possess native three-dimensional structures, can’t perform their
physiological functions
○ Caused by organic solvents, heavy metal ions, high concentrations of inorganic salts,
changes In pH + temperature

● Tertiary structure
● 6 interactions
○ Hydrogen bonding
○ Hydrophobic interactions/van der Waals
○ Disulphite bridges
○ Amide linkages
○ Ester bonds
■ o ​Ionic bonds

Enzymes
● Chemical recognition occurs
● Efficiency of enzyme depends on the configuration and charge of its active site
● Amino acid residues of the enzyme backbone and active site contain ionisable side-chains
that undergo reversible protonation or deprotonation
● Change in pH affects the charges of the ionisable side-chains and their ability to form ionic
and hydrogen bonds with one another
● Weakening and breaking of bonds alter the structure and shape of active site
● Substrate contains ionisable functional groups that must have specific charges in order to
interact with the active site
● Heavy metal ions (e.g. lead II, mercury II, cadmium II)
○ preferentially bind to -SH groups in the side chains of cysteine residues
○ This disrupts the formation of disulphide bridges
○ They can also replace them with sulphur-metal-sulphur fragments
○ Primary cause of heavy metal toxicity
 ○ Can also be components of prosthetic groups

Enzyme kinetics – Michaelis-Menten plot

● When substrate concentration is low, reaction rate (v) is proportional to substrate
concentration ([S]) ​→​first order reaction in respect to S
○ The beginning (linear increase) of the enzymatic reaction
● When substrate concentration is high, v is nearly independent of [S] ​→​zero order reaction
with respect to S
○ The plateau (saturation) of the enzymatic reaction

●
● A substrate molecule must remain at the active site for a certain period of time, and so the
enzyme is unavailable for other substrate molecules
● When [S] is high all active sites are occupied
● When [S] is low every substrate molecule can bind to the nearest enzyme without delay

Non-competitive inhibition
● Allosteric sites can be temporarily binded to specific molecules via weak non-covalent
interactions

B.3 lipids 
● Non-polar
● Insoluble in water
● Functions: energy storage, chemical messaging, chemical transport, thermal
insulation, physical separation of cell content from biological fluids
● Hydrophobic
● Held by weak van der Waals’s forces
 ● Naturally occurring unsaturated fatty acids = cis
● Unwanted by-products in food processing = trans-fatty acids
● Mixed triglycerides contain residues of two or three different fatty acids
● Saturated triglycerides are solid at room temperature
○ Straight hydrocarbon chains
○ Can pack closely together and form multiple van der Waals’ interactions with
one another
● Fatty acid + glycerol → triglyceride + water, ester bond

Iodine number 
● Degree of unsaturation​: the average number of C=C bonds per unit mass of fat/oil
● Degree of unsaturation can be determined by a reaction of a triglyceride mixture with
elemental iodine that combines C=C bonds by ​electrophilic addition
● Iodine number​: the maximum mass of iodine in grams that can be consumed by 100g of
triglyceride
● Mixture turns yellow-brown ​→​reaction is complete, all C=C bonds have reacted with iodine

Rancidity of fats 
● Hydrolytic rancidity is caused by the hydrolysis of ester bonds when food is exposed to
moisture
● Hydrolysis accelerated by enzymes, organic acids, and high temperatures
● Oxidative rancidity
○ More double bonds = more likely to become rancid
○ Free radical reactions, free radical oxidation

Health 
Polyunsaturated fatty acids are healthier because they:
● Decrease the risk of atherosclerosis
● Decrease the risk of heart disease
● Decreases the risk of cardiovascular disease
● Less likely to be deposited on walls of arteries (than saturated fatty acids)

Calculating energy content 

● The released energy is absorbed by the water
● The released energy can be calculated from the temperature change, mass of water, and
heat capacity

Phospholipids 
● Triglycerides except one phospholipid is replaced by a phosphate group with a phosphate
ester bond (instead of a normal ester bond)
● Polar phosphate group + 2 non-polar hydrocarbon chains = amphiphilic phospholipid
○ Both hydrophobic (tails) and hydrophilic (heads)
○ Maximises van der Waals’ interactions
 ○ Allows hydrophilic heads to form H bonds and dipole-dipole interactions with water
and each other
○ Hydrophobic nature makes phospholipid bilayers impermeable to ions and polar
molecules. Proteins and steroids embedded in cell membranes allow controlled
transport of ions, nutrients, and metabolites

Steroids
· Steroidal backbone
· E.g. Cholesterol
o ​Essential to cell membranes
o ​LDLs carry more cholesterol than HDLs

Saponification
· Alkaline hydrolysis of fats
· Fat is treated with hot solution of sodium hydroxide
· Sodium salt of fatty acid is separated by precipitation
· Produces soap bars
· KOH soaps are used in liquid detergents due to low melting points

Boiling points 
Fatty acids have higher boiling points when:
● Chain has no kinks/more regular structure
● Straight chain
● No C=C/carbon to carbon double bonds
● Saturated
● Chains pack more closely together

B.5 Vitamins 
·​ ​They are ​micronutrients​ – substances required in very small amounts
·​ ​Mainly cofactors of enzymes

·​ ​Fat soluble vitamins

o​ ​Long, non-polar chains / rings

o​ ​ADEFK
·​ ​Water soluble

o​ ​Polar groups
o​ ​BC
·​ ​Vitamin A – Retinol

o​ ​Lack can cause night blindness

·​ ​Fe

o​ ​Anemia
·​ ​Vitamin C – Ascorbic acid

o​ ​Lack of it can cause scurvy, which has the following symptoms:

o​ ​Swollen legs
o​ ​Rotten gums
o​ ​Bloody lesions
·​ ​Vitamin D – Calciferol
o​ ​Aids in absorption of calcium
o​ ​Lack can cause osteoporosis – frail bones
o​ ​Also can cause rickets – bone deformation
·​ ​Solutions

o​ ​Eating fresh foods rich in vitamins and minerals

o​ ​GM foods
o​ ​Nutritional supplements

UV - Vis
● Cancer
● Protein assays – methods of measuring the concentration of protein in a sample
● Tests via visible and ultraviolet light
● When UV-vis is performed, an ​absorption spectrum​ is created

From past papers 

B2 proteins 

State five different types of interactions that can occur between 2-amino acids to give a three
dimensional state. In each case, identify the atoms or groups joined together.
● Van der Waals attraction between nonpolar groups
● Ionic bonding between charged groups/NH3+ and COO-
● Hydrogen bonding between H bonded to O or N with another O or N
● Disulfide bridges/bonds between two S atoms (in cysteine)
● Peptide linkages/bonds between -COOH and -NH2 groups

Outline the significance of the value of Km

● Km is inverse measure of affinity of enzyme for a substrate/Km is inversely
proportional to enzyme activity
● High value of Km indicates higher substrate concentration needed for enzyme
saturation
● Low value of Km means reaction is fast at low substrate concentration

Why would amino acids develop close to the negative electrode?

● pH < pI
● Buffer more acidic than amino acid (at isoelectric point)
● Amino acid positively charged so moves towards negative electrode

Comment on the rate of reaction at optimum temperature in terms of the enzyme’s active
site
● Highest frequency of successful collisions between active site and substrate
● Highest frequency of collisions between active site and substrate with sufficient
energy/E>Ea and correct orientation/conformation
● Optimal shape/conformation of the active site (that matches the substrate)
 ● Best ability of the active site to bind (to the substrate)
Outline how the presence of heavy metal ions decreases the action of enzymes
● react/bind/chelate with enzyme
● Disrupt ionic salt bridges
● Affect shape of tertiary/quaternary structures
● Precipitate enzymes
● break/disrupt disulfide bridges/bonds

Outline the action of a non-competitive inhibitor on the enzyme-catalysed reaction

● Does not compete for active site
● Binds to allosteric site/away from (enzyme) active site
● Alters shape of enzyme
● Reduces rate/Vmax

B3 lipids 

Fatty acids react with glycerol to form fats and oils. What’s the chemical link formed called?
● Ester bond

Fatty acid + glycerol → triglyceride. What’s the other product?

● Water

Solid fat triglycerides can clog kitchen sink drains. Explain how sodium hydroxide unblocks
the drain.
● (base) hydrolysis/saponification
● (produces glycerol and) soap/salt of the fatty acid

B5 vitamins 

Vision is dependent on retinol (vitamin A) present in retina cells. Retinol is oxidized to the
photosensitive chemical 11-cis-retinal and isomerizes to 11-trans-retinal on absorption of
light. Outline how the formation of 11-trans-retinal results in the generation of nerve signals
to the brain.
● 11-trans retinal no longer fits into the rhodopsin/protein OR 11-trans retinal is ejected
from the rhodopsin/protein leads to conformational change in rhodopsin/protein «to
opsin generating signals»

Nucleic acids 

Explain the shape of the beginning of the pO2 curve at low oxygen partial pressure
● Oxygen binds to first active site (of deoxygenated heme) ​and​ alters shape of other
active sites
● Cooperative binding
● Affinity of partially oxygenated hemoglobin for oxygen increases
Notes 
● Ascorbic acid/vitamin C is the most soluble
● Decreasing pH decreases oxygen saturation of hemoglobin
● Ozone absorbs IR and oxygen doesn’t
● Alkenyl is an open fragment of an alkene
● 3 6C rings and 1 5C ring/fused ring structure/four-ring backbone = steroid

OPTION C: ENERGY 
(theres two sets of notes here in some parts btw - naina)

C.1 - Energy sources 

● energy has both quantity and quality
● a useful energy source release energy at a reasonable rate and produces minimal
pollution
● energy density = energy released/volume of fuel (kJ/dm3)
● specific energy = energy release/mass of fuel (kJ/kg)
● energy density = specific energy * density
● efficiency of energy transfer = (useful energy output/total energy output) * 100

C.2 - Fossil fuels 

● octane number: resistance of knocking in car engines
● knocking: autoignition of fuels
○ damages engines
○ indicates low fuel efficiency
● 2,2,4-trimethylpentane has an octane number of 100
● heptane has an octane number of 0
● petrol has an octane number of 93 - same tendency to auto-ignite as 93%
2,2,4-trimethylpentane and 7% heptane
● more branching - higher octane number - more efficient
● short-chain/cyclic/aromatic - high octane numbers
● octane number increases with a decrease in carbon chain length
● octane number increases with increased carbon chain branching
● octane number increases in aromatic hydrocarbons and cyclic hydrocarbons
● reforming changes straight-chain hydrocarbons to compounds containing benzene
rings
○ catalyst: platinum
○ temperature: 500C
○ pressure: 20 atm
● isomerism: straight chain - branched chain
○ catalyst: platinum or zeolite
 ● knocking is caused by a fuel’s tendency to auto-ignite
● a measure of the fuel’s ability to resist auto-ignition is its octane number
○ 2,2,4-trimethylpentane has an octane number of 100
○ hexane has an octane number of 0
● hydrocarbon fuels can be improved by cracking and catalytic reforming reactions
● catalytic reforming involves molecular rearrangement
○ straight-chain carbons are converted to branched-chain or cyclic compounds
● carbon footprint is the total amount of greenhouse gases produced during human
activities
○ it is expressed in terms of CO2 produced
● coal gasification: C + H2O -> CO + H2
● coal liquefaction: nCO + (2n+1)H2 -> C(n)H(2n+2) + nH2O

C.3 - Nuclear fusion and fission 

● nuclear fusion: deuterium + tritium -> helium + neutron + energy
● nuclear fusion: 235-U + neutron -> 141-Ba + 92-Kr + 3 neutrons + energy
● nuclear fusion occurs in stars
● nuclear fission is used in bombs and nuclear reactors
● safety issues: health, nuclear weapons, core meltdown
 ● binding energy is the energy required to disassemble an atomic nucleus to its
component parts (nucleons)
○ the binding energy curve indicates the stability of atoms
○ the higher the curve the more stable the nucleus
● the half-life of a radioisotope is the time taken for the radioactive nuclei to decay to
half of its original mass
○ half-life = time * (ln2/ln (original mass/new mass))
○ original mass = new mass * 2^number of half-lives passed
● short half-life = high radioactivity
● low-level nuclear waste - present in items used during cancer treatment (gloves,
papers, etc.)
● decay constant (​λ​) is the inverse of the mean lifetime (average lifetime of a
radioactive particle before decay)
○ half-life = ln2 / ​λ
● breeder-reactor- nuclear reactor that produces more fission material than it
consumes
○ fission material is capable of sustaining a nuclear reaction
● fast breeder reactors were developed because the supply of fissile 235-U is limited
● non fissile 238-U is much more abundant than fissile 235-U
● Pu-239, used as a fuel in breeder reactions, is produced from U-235 by neutron
capture

C.4 - Solar energy 

●

● light can be absorbed by chlorophyll and other pigments with conjugated electronic
structure (alternating C-C and C=C bonds)
● aerobic respiration: 6O2 + C6H12O6 -> 6CO2 + 6H2O
● anaerobic respiration: C6H12O6 -> 2C2H5OH + 2CO2
● photosynthesis: 6CO2 + 6H2O -> C6H12O6 + 6O2
● transesterification: RCOOR’ + R’’OH -> RCOOR’’ + R’OH
○ catalyst: strong base (eg. NaOH)
C.5 - Environmental impact - global warming

C.6 - Electrochemistry, rechargeable batteries and fuel cells (AHL)

C.7 - Nuclear fusion and nuclear fission (AHL)

C.8 - Photovoltaic cells and dye-sensitized solar cells (AHL)

PAST PAPER QUESTIONS 

Periodicity 
Define the term ​first ionisation energy
minimum energy required to remove one electron / energy required to remove most
loosely bound/outermost electron;
from gaseous/isolated atom;

Bonding 
Define the term ​average bond enthalpy
The average amount of energy needed to break a specific type of bond, measured over a
wide variety of different gaseous molecules.

Equilibrium 
 

As we can see, the moles of Na2So4 is 0.1

And we also know that the molar ratios across all components are 1
Which means, the reactants moles must also be equal to the amount of moles of that
reactant Na2So4
Which means, We must find the missing molar mass, which is molar mass of Na2So4 + x
So the overall equation would be 32.2 / (142 + x*18) =0.1
Hence, X is 10

Acids and bases 

 
The answer is B because H​2​SO​4​ is diprotic (2 Hs) thus will generate twice the amount of
heat

Organic chemistry 
Optically active compound
● Chiral/asymmetric center
● C-atoms that have 4 different groups bonded to them/mirror image identical to
original molecule

The compound above is isomeric with hexane. Predict, giving reasons, how the boiling
points of these compounds would compare.
● Compound lower/hexane higher and van der Waals’/London/dispersion forces
between molecules weaker in compound/stronger in hexane
● Compound is more branched/has a lower surface area/has a more spherical
shape/does not pack as closely

Q: explain why monomers are often gases or volatile liquids, but polymers are solids
● Monomers are smaller molecules/have a smaller surface area than larger molecules
● With weaker Van der Waals’/London/dispersion forces

C5H12 and C5H11OH: which produces more heat in complete combustion and why
● C5H12
● C5h11oh has a higher molar mass/produces less grams of CO2 and h2o per gram of
the compound
● O contributes nothing to energy released/partially oxidised
● Bond strength in pentanol higher than pentane
● Pentanol requires more energy to break intermolecular forces/H bonding
Notes from pps:
● Polymerisation is an addition reaction (could also be condensation)
● Hydrogen bonds are NOT vdw forces
● Alcohol + carboxylic acid → ester

Nature of science 

For covalents, all the oxidation states SHOULD be negative because they’re all gaining
electrons from shared pairs. The question is asking why they’re positive, and it’s because
oxidation states are only used theoretically.