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The Henderson–Hasselbalch equation can be used to estimate the pH of a buffer solution by approximating the actual concentration ratio as the ratio of the analytical concentrations of the acid and of a salt, MA. The equation can also be applied to bases by specifying the protonated form of the base as the acid.
A strong acid, such as hydrochloric acid, at concentration 1 mol dm −3 has a pH of 0, while a strong alkali like sodium hydroxide, at the same concentration, has a pH of 14. Since pH is a logarithmic scale, a difference of one in pH is equivalent to a tenfold difference in hydrogen ion concentration.
Speciation of ions refers to the changing concentration of varying forms of an ion as the pH of the solution changes. [1]The ratio of acid, AH and conjugate base, A −, concentrations varies as the difference between the pH and the pK a varies, in accordance with the Henderson-Hasselbalch equation.
In practice, the mixture can be created by dissolving the acid in water, and adding the requisite amount of strong acid or base. When the pK a and analytical concentration of the acid are known, the extent of dissociation and pH of a solution of a monoprotic acid can be easily calculated using an ICE table.
In the case of citric acid, the overlap is extensive and solutions of citric acid are buffered over the whole range of pH 2.5 to 7.5. Calculation of the pH with a polyprotic acid requires a speciation calculation to be performed. In the case of citric acid, this entails the solution of the two equations of mass balance:
The isohydric principle is the phenomenon whereby multiple acid/base pairs in solution will be in equilibrium with one another, tied together by their common reagent: the hydrogen ion and hence, the pH of solution. That is, when several buffers are present together in the same solution, they are all exposed to the same hydrogen ion activity.
The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The p K a values of an amino acid side chain in solution is typically inferred from the p K a values of model compounds (compounds that are similar to ...
The concentration of water, [H 2 O], is omitted by convention, which means that the value of K w differs from the value of K eq that would be computed using that concentration. The value of K w varies with temperature, as shown in the table below. This variation must be taken into account when making precise measurements of quantities such as pH.