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pKa values for acetic, chloroacetic, dichloroacetic and trichloroacetic acids. Inductive effects and mesomeric effects affect the p K a values. A simple example is provided by the effect of replacing the hydrogen atoms in acetic acid by the more electronegative chlorine atom.
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.
In computational biology, protein pK a calculations are used to estimate the pK a values of amino acids as they exist within proteins.These calculations complement the pK a values reported for amino acids in their free state, and are used frequently within the fields of molecular modeling, structural bioinformatics, and computational biology.
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.
A buffer solution is a solution where the pH does not change significantly on dilution or if an acid or base is added at constant temperature. [1] Its pH changes very little when a small amount of strong acid or base is added to it.
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.
PKA is one of the most widely researched protein kinases, in part because of its uniqueness; out of 540 different protein kinase genes that make up the human kinome, only one other protein kinase, casein kinase 2, is known to exist in a physiological tetrameric complex, meaning it consists of four subunits. [1]
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]