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Conversely, when pH = pK a, the concentration of HA is equal to the concentration of A −. The buffer region extends over the approximate range pK a ± 2. Buffering is weak outside the range pK a ± 1. At pH ≤ pK a − 2 the substance is said to be fully protonated and at pH ≥ pK a + 2 it is fully dissociated (deprotonated).
From the titration of protonatable group, one can read the so-called pK a 1 ⁄ 2 which is equal to the pH value where the group is half-protonated (i.e. when 50% such groups would be protonated). The pK a 1 ⁄ 2 is equal to the Henderson–Hasselbalch pK a (pK HH a) if the titration curve follows the Henderson–Hasselbalch equation. [14]
The converse is true in a basic medium. For example, Naproxen is a non-steroidal anti-inflammatory drug that is a weak acid (its pKa value is 5.0). The gastric juice has a pH of 2.0. It is a three-fold difference (due to log scale) between its pH and its pKa; therefore there is a 1000× difference between the charged and uncharged concentrations.
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 pH of a solution of a monoprotic weak acid can be expressed in terms of the extent of dissociation. After rearranging the expression defining the acid dissociation constant, and putting pH = −log 10 [H +], one obtains pH = pK a – log ( [AH]/[A −] ) This is a form of the Henderson-Hasselbalch equation. It can be deduced from this ...
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. Buffer solutions are used as a means of keeping pH at a nearly constant value in a wide variety of chemical ...
If the pH of the buffer is below the pI of the protein being run, the protein will migrate to the negative pole of the gel (positive charge is attracted to the negative pole). If the protein is run with a buffer pH that is equal to the pI, it will not migrate at all. This is also true for individual amino acids.
The Henderson–Hasselbalch equation can be used to model these equilibria. It is important to maintain this pH of 7.4 to ensure enzymes are able to work optimally. [10] Life threatening Acidosis (a low blood pH resulting in nausea, headaches, and even coma, and convulsions) is due to a lack of functioning of enzymes at a low pH. [10]