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.
Current pH
—
- Titrant added
- —
- pKa (region)
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- Equivalence volume Veq
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- Half-equivalence Veq/2
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- Buffer capacity β
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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.