pKa Calculation Principle:
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pKa is the negative logarithm of the acid dissociation constant (Ka). It represents the pH at which half of the acid molecules are dissociated and half are undissociated. A lower pKa value indicates a stronger acid.
The pKa can be determined from a pH titration curve by identifying the pH value at the half-equivalence point:
Where:
Explanation: At the half-equivalence point of a weak acid titration, exactly half of the acid has been neutralized by base. At this point, the concentrations of the acid and its conjugate base are equal, making pH = pKa.
Details: pKa values are crucial for understanding acid-base chemistry, predicting reaction outcomes, designing pharmaceutical compounds, and understanding biochemical processes. They help determine the extent of ionization of compounds at different pH levels.
Tips: Enter the pH value measured at the half-equivalence point of your titration curve. The value must be between 0-14 pH units. The calculator will return the pKa value which is numerically equal to the pH at this point.
Q1: Why is pKa equal to pH at half-equivalence point?
A: According to the Henderson-Hasselbalch equation, when [HA] = [A⁻], the log term becomes zero, making pH = pKa.
Q2: What is the typical range of pKa values?
A: pKa values typically range from -10 to 50, with most common acids falling between 0-14. Strong acids have negative pKa values, while weak acids have positive values.
Q3: Can this method be used for polyprotic acids?
A: Yes, for polyprotic acids, each equivalence point corresponds to a different pKa value. The first half-equivalence point gives pKa₁, the second gives pKa₂, etc.
Q4: What factors affect pKa determination accuracy?
A: Temperature, ionic strength, and measurement precision can affect the accuracy. The titration should be performed under controlled conditions for best results.
Q5: How does pKa relate to buffer capacity?
A: Maximum buffer capacity occurs when pH = pKa. Buffers are most effective within ±1 pH unit of their pKa value.