All guides
Every long-form tutorial we've published, grouped by discipline. Each guide is self-contained, cited to primary sources, and typically 10 to 15 minutes to read.
General chemistry
Everyday lab math — molarity, dilutions, molar mass, buffers, and serial dilutions. The bench toolkit every chemist reaches for daily.
- Stoichiometry: how to think in moles
The mole map, limiting reagents, and the cascading errors that ruin a synthesis calc — with three worked problems.
- Limiting reagent, deeply
It is not the smallest number of moles — it is the reagent that runs out first at the reaction ratio. The three-column method that never fails.
- Percent yield accounting: where the mass went
Theoretical yield is a ceiling, actual yield is the receipt, and the gap between them is where the chemistry actually happened.
- Concentrations decoded: mass %, molality, ppm
Molarity is one of six ways to say 'how concentrated'. Mass percent, molality, ppm, mole fraction — each has a job.
- The ideal gas law: PV=nRT and where it breaks
Four variables, one line — until temperature drops or pressure climbs. Boyle, Charles, Avogadro, and the van der Waals correction that patches the damage.
- Balancing redox equations: the half-reaction method
Split the equation in two, balance atoms, balance charge with electrons, add. A seven-step algorithm that never fails, in acid or in base.
- Colligative properties: the four that matter
Vapour-pressure lowering, boiling-point elevation, freezing-point depression, osmotic pressure — four properties, one common cause: lowered solvent chemical potential.
Organic chemistry
Reaction mechanisms, functional-group transformations, NMR and IR interpretation, stereochemistry, and yield accounting for synthesis routes.
- SN1 vs SN2 in five decisions
Substrate, nucleophile, leaving group, solvent, temperature — a five-way decision tree that predicts which mechanism wins.
- E1 vs E2 vs substitution: the full decision map
Four mechanisms compete on the same substrate. Sort reagents on two axes, substrates on one, and the answer falls out.
- Electrophilic addition: Markovnikov and the rearrangements
Alkenes are electron-rich; electrophiles love them. Markovnikov, anti-Markovnikov exceptions, and cation rearrangements that flip the product.
- Reading an NMR spectrum: shift, integration, splitting
The proton NMR spectrum is a compressed structure drawing. Three independent axes identify a molecule from scratch.
- Aromaticity: Hückel's rule and benzene reactivity
Six π electrons, one flat ring, one enormous energy discount. The four criteria for aromaticity and how they control reactivity.
- Carbonyl chemistry: additions and eliminations
Half of organic chemistry is one polarised π bond. Aldehyde and ketone additions, acyl-derivative substitutions, and the reactivity ladder.
- The Diels-Alder reaction: reading a cycloaddition
Diene plus dienophile equals cyclohexene in one concerted step. FMO theory, endo rule, and the stereo constraints that make it a synthesis workhorse.
Inorganic chemistry
Coordination chemistry, oxidation-state bookkeeping, crystal-field splitting, and solid-state stoichiometry.
- Reading a solubility table without memorizing it
The three families that cover 90 percent of solubility questions, the classic exceptions, and how to spot them at a glance.
- Ksp: from rules to numbers
Move from 'insoluble' to a real molar solubility, then correct for the common-ion effect, pH, and selective precipitation.
- Crystal field theory: predicting color and magnetism
d-orbital splitting, Δo, high-spin vs low-spin, and how one diagram predicts a complex's color, magnetic moment, and geometry.
- The 18-electron rule and organometallic bookkeeping
Transition metals like to have 18 valence electrons. Count them right and half of organometallic reactivity falls out.
- MO theory for diatomic molecules
Bond order, magnetism, and bond length fall out of one MO diagram. Build it once for the first row and every diatomic follows.
- Reading a Latimer diagram: redox at a glance
One line shows every oxidation state and every E° between them. Read forward for stability, backward for disproportionation, both for oxidiser strength.
- Point groups and molecular symmetry
Every molecule belongs to a point group. The five symmetry elements identify it; the group then predicts polarity, chirality, and spectral activity.
Physical chemistry
Thermodynamics, kinetics, and equilibrium — gas laws, Gibbs free energy, Arrhenius kinetics, and rate-law analysis.
- What entropy actually is
Boltzmann's S = k ln W, worked out on a microstate count you can do by hand. Why 'disorder' is a lossy metaphor.
- Gibbs free energy in three intuitions
Universe's entropy proxy, max non-PV work, distance from equilibrium — three framings of ΔG that each earn their keep.
- Rate laws from mechanism up
Rate laws come from mechanism, not the balanced equation. Elementary steps, RDS, steady-state, integrated rate laws — and when to trust them.
- Transition state theory: the Eyring equation
Arrhenius fits the rate; Eyring names the reason. ΔH‡ and ΔS‡ split 'why so slow' into an enthalpic hill and an entropic bottleneck.
- Phase diagrams: reading pressure-temperature maps
One diagram encodes every phase transition a pure substance can undergo. The three lines are Clapeyron; the intersections carry the physics.
- The Boltzmann distribution: populations at temperature
Two energy levels, one temperature — one exponential fixes the ratio. IR intensities, NMR sensitivity, and the molecular meaning of T all follow.
- The particle in a box: the simplest quantum problem
One particle, one 1D box, one exact solution. Quantised energies, zero-point energy, and a working model for the absorption of conjugated polyenes.
Analytical chemistry
Titration curves, pH and normality of acid–base systems, Beer–Lambert absorbance, chromatography retention, and calibration regression.
- When Beer-Lambert lies
Concentration limits, scattering, stray light, chemical speciation — the five ways the A = εbc line stops being a line.
- Calibration curves without lying to yourself
Build a regression that survives an audit: LOD, LOQ, confidence interval, residual plot, and when to switch to standard addition.
- Reading titration curves: what the shape tells you
Buffer plateaus, equivalence points, and half-equivalence-point pH — the shape of the curve names the analyte and gives the pKa for free.
- Reading an HPLC chromatogram: retention and resolution
Retention, plate count, resolution, peak shape — the four numbers that grade any HPLC separation.
- Reading a mass spectrum: fragments and isotopes
The molecular ion names the mass; the fragment pattern names the connectivity; the isotope satellites name the elements.
- IR spectroscopy: reading the functional-group region
The 4000-1500 window names the functional groups; the fingerprint below 1500 confirms the identity. A four-question workflow reads any spectrum.
- Analytical statistics: mean, SD, and the t-test
Every measurement is a random variable. Mean, standard deviation, standard error, confidence interval, t-test, and outlier rejection — in one workflow.
Biochem chemistry
Enzyme kinetics (Michaelis–Menten, Lineweaver–Burk), protein–ligand binding, nucleic-acid Tm, and biological buffer preparation.
- Why enzymes plateau: reading v vs [S] curves
Michaelis-Menten in words. What Km and Vmax actually mean, and what kcat/Km tells you about a 'perfect' enzyme.
- Reading enzyme inhibition patterns
Each inhibition mode leaves a distinct Km/Vmax fingerprint. Match the pattern, extract Ki, watch for irreversibility.
- Physiological buffers: beyond Henderson-Hasselbalch
Bicarbonate, phosphate, and protein buffers keep blood pH within 0.05 units. The 20:1 ratio, the open system, and the four ABG disturbances.
- Cooperative binding: hemoglobin and the Hill equation
Hemoglobin binds four oxygens, and each binds easier than the last. The Hill equation, MWC states, and the Bohr effect.
- Bioenergetics: ΔG in a metabolic pathway
ATP is not the fuel; ΔG is. Every step has a ΔG, and only the sum needs to be negative. How coupling and disequilibrium drive the pathway.
- Electron transport chain: proton gradient to ATP
Four complexes drop electrons through a redox staircase to O₂; the released energy pumps protons; ATP synthase turns the gradient back into ATP.
- Membrane transport: passive, facilitated, and active
Three transport modes set every ion gradient in every cell. Nernst equation, Na/K-ATPase, secondary active symporters and antiporters, and the physiology that rides them.