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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.
Species concentrations calculated with the program HySS for a 10 mM solution of citric acid. pK a1 = 3.13, pK a2 = 4.76, pK a3 = 6.40. 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 ...
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 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 ...
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Buffer capacity falls to 33% of the maximum value at pH = pK a ± 1, to 10% at pH = pK a ± 1.5 and to 1% at pH = pK a ± 2. For this reason the most useful range is approximately pK a ± 1. When choosing a buffer for use at a specific pH, it should have a pK a value as close as possible to that pH. [2]