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Well measured values are typically within 0.1 units of each other. Data presented here were taken at 25 °C in water. [7] [86] More values can be found in the Thermodynamics section, above. A table of pK a of carbon acids, measured in DMSO, can be found on the page on carbanions.
See Amino acid for the pK a values of all amino acid side chains inferred in such a way. There are also numerous experimental studies that have yielded such values, for example by use of NMR spectroscopy. The table below lists the model pK a values that are often used in a protein pK a calculation, and contains a third column based on protein ...
The following table presents pK a values at 20 °C. Values change by about 0.01 per degree of temperature. [1] [3] Good's original 1966 paper had two older buffers (marked with italics) for comparison. In 1972 Good published a second list with three more buffers, and five more were added in 1980.
In cell biology, protein kinase A (PKA) is a family of serine-threonine kinase [1] whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase (EC 2.7.11.11). PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism.
In the case of multiple pK values they are designated by indices: pK 1, pK 2, pK 3 and so on. For amino acids, the pK 1 constant refers to its carboxyl (–COOH) group, pK 2 refers to its amino (–NH 2) group and the pK 3 is the pK value of its side chain.
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The difference between successive pK a values is sufficiently large so that salts of either monohydrogen phosphate, HPO 2− 4 or dihydrogen phosphate, H 2 PO − 4, can be prepared from a solution of phosphoric acid by adjusting the pH to be mid-way between the respective pK a values.
Acid strength is the tendency of an acid, symbolised by the chemical formula HA, to dissociate into a proton, H +, and an anion, A −.The dissociation or ionization of a strong acid in solution is effectively complete, except in its most concentrated solutions.