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pKa values for acetic, chloroacetic, dichloroacetic and trichloroacetic acids. Inductive effects and mesomeric effects affect the pK a values. A simple example is provided by the effect of replacing the hydrogen atoms in acetic acid by the more electronegative chlorine atom.
pK a values of amino acid side chains play an important role in defining the pH-dependent characteristics of a protein. 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.
Citric acid is a triprotic acid, with pK a values, extrapolated to zero ionic strength, of 3.128, 4.761, and 6.396 at 25 °C. [21] The pK a of the hydroxyl group has been found, by means of 13 C NMR spectroscopy, to be 14.4. [22] The speciation diagram shows that solutions of citric acid are buffer solutions between about pH 2 and pH 8. In ...
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.
Acid strength is the tendency of an acid, symbolised by the chemical formula, to dissociate into a proton, +, and an anion, .The dissociation or ionization of a strong acid in solution is effectively complete, except in its most concentrated solutions.
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.
In chemistry, biochemistry, and pharmacology, a dissociation constant (K D) is a specific type of equilibrium constant that measures the propensity of a larger object to separate (dissociate) reversibly into smaller components, as when a complex falls apart into its component molecules, or when a salt splits up into its component ions.
The pKa of KHP is 5.4, so its pH buffering range would be 4.4 to 6.4; however, due to the presence of the second acidic group that bears the potassium ion, the first pKa also contributes to the buffering range well below pH 4.0, which is why KHP is a good choice for use as a reference standard for pH 4.00. [8] [9]