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In chemistry and biochemistry, the Henderson–Hasselbalch equation = + ([] []) relates the pH of a chemical solution of a weak acid to the numerical value of the acid dissociation constant, K a, of acid and the ratio of the concentrations, [] [] of the acid and its conjugate base in an equilibrium.
Therefore, the buffer regions will be centered at about pH 1.3 and pH 4.3. The buffer regions carry the information necessary to get the pK a values as the concentrations of acid and conjugate base change along a buffer region. Between the two buffer regions there is an end-point, or equivalence point, at about pH 3.
A weak acid may be defined as an acid with pK a greater than about −2. An acid with pK a = −2 would be 99 % dissociated at pH 0, that is, in a 1 M HCl solution. Any acid with a pK a less than about −2 is said to be a strong acid. Strong acids are said to be fully dissociated.
The measurement of pH can become difficult at extremely acidic or alkaline conditions, such as below pH 2.5 (ca. 0.003 mol/dm 3 acid) or above pH 10.5 (above ca. 0.0003 mol/dm 3 alkaline). This is due to the breakdown of the Nernst equation in such conditions when using a glass electrode. There are several factors that contribute to this problem.
The first (e.g., acetic acid or ammonium) have only one dissociable group, the second (e.g., carbonic acid, bicarbonate, glycine) have two dissociable groups and the third (e.g., phosphoric acid) have three dissociable groups. In the case of multiple pK values they are designated by indices: pK 1, pK 2, pK 3 and so on.
The Hammett acidity function (H 0) is a measure of acidity that is used for very concentrated solutions of strong acids, including superacids.It was proposed by the physical organic chemist Louis Plack Hammett [1] [2] and is the best-known acidity function used to extend the measure of Brønsted–Lowry acidity beyond the dilute aqueous solutions for which the pH scale is useful.
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 ...
A typical titration curve of a diprotic acid, oxalic acid, titrated with a strong base, sodium hydroxide.Both equivalence points are visible. Titrations are often recorded on graphs called titration curves, which generally contain the volume of the titrant as the independent variable and the pH of the solution as the dependent variable (because it changes depending on the composition of the ...