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Buffer capacity falls to 33% of the maximum value at pH = pK a ± 1, to 10% at pH = pK a ± 1.5 and to 1% at pH = pK a ± 2. For this reason the most useful range is approximately pK a ± 1. When choosing a buffer for use at a specific pH, it should have a pK a value as close as possible to that pH. [2]
The Henderson–Hasselbalch equation can be used to estimate the pH of a buffer solution by approximating the actual concentration ratio as the ratio of the analytical concentrations of the acid and of a salt, MA. The equation can also be applied to bases by specifying the protonated form of the base as the acid.
The equilibrium state is represented by the equation: + + If α is the fraction of dissociated electrolyte, then αc 0 is the concentration of each ionic species. (1 - α) must, therefore be the fraction of undissociated electrolyte, and (1 - α)c 0 the concentration of same. The dissociation constant may therefore be given as
In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
Hence, the pK of each buffer will dictate the ratio of the concentrations of its base and weak acid forms at the given pH, in accordance with the Henderson-Hasselbalch equation. Any condition that changes the balance of one of the buffer systems, also changes the balance of all the others because the buffer systems actually buffer one another ...
A thermal shift assay (TSA) measures changes in the thermal denaturation temperature and hence stability of a protein under varying conditions such as variations in drug concentration, buffer formulation (pH or ionic strength), redox potential, or sequence mutation. The most common method for measuring protein thermal shifts is differential ...
The bicarbonate buffer system is an acid-base homeostatic mechanism involving the balance of carbonic acid (H 2 CO 3), bicarbonate ion (HCO − 3 ), and carbon dioxide (CO 2 ) in order to maintain pH in the blood and duodenum , among other tissues, to support proper metabolic function. [ 1 ]