Experiment 2 · Titration Curve Simulator

Add a strong base (or acid) to a weak acid and watch the pH curve form. Find the buffering region, the half-equivalence point (where pH = pKa), and the equivalence point.

The strong reagent in the burette.
Titrant type
0.0 mL
Drag to dose, or animate the whole titration.

Current pH
Titrant added
pKa (region)
Equivalence volume Veq
Half-equivalence Veq/2
Buffer capacity β
The curve is flattest — and the buffer capacity β is largest — right at pH = pKa (the half-equivalence point). That is the heart of the buffering region, roughly pKa ± 1.

Teaching model: activity is treated as equal to concentration and ionic-strength effects are ignored. Each buffer is modelled with a single relevant pKa, and the strong titrant is assumed fully dissociated. Real titration curves shift a little with ionic strength and (for polyprotic acids) show extra features.