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At half-neutralization the ratio [A −] / [HA] = 1; since log(1) = 0, the pH at half-neutralization is numerically equal to pK a. 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.
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 ] Most p K a calculation methods silently assume that all titration curves are Henderson–Hasselbalch shaped, and p K a values in p K a calculation programs are therefore often determined in this way.
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 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.
When the acidic medium in question is a dilute aqueous solution, the is approximately equal to the pH value, which is a negative logarithm of the concentration of aqueous + in solution. The pH of a simple solution of an acid in water is determined by both K a {\displaystyle K_{{\ce {a}}}} and the acid concentration.
The last few weeks of the year can be a busy and stressful time. Here’s how to focus on what really matters this holiday season, according to experts.
The search for a woman who is believed to have fallen into a sinkhole in western Pennsylvania has become a recovery effort after two treacherous days of digging through mud and rock produced no ...
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.