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Between the two buffer regions there is an end-point, or equivalence point, at about pH 3. This end-point is not sharp and is typical of a diprotic acid whose buffer regions overlap by a small amount: pK a2 − pK a1 is about three in this example. (If the difference in pK values were about two or less, the end-point would not be noticeable ...
The dissociation constant is commonly used to describe the affinity between a ligand (such as a drug) and a protein; i.e., how tightly a ligand binds to a particular protein. Ligand–protein affinities are influenced by non-covalent intermolecular interactions between the two molecules such as hydrogen bonding , electrostatic interactions ...
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.
Bjerrum plot of speciation for a hypothetical monoprotic acid: AH concentration as a function of the difference between pK and pH. Carbonic acid is the formal Brønsted–Lowry conjugate acid of the bicarbonate anion, stable in alkaline solution. The protonation constants have been measured to great precision, but depend on overall ionic ...
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.
The difference between the two, therefore, is the quantity of charged sites at the point of net zero charge. Jolivet uses the intrinsic surface equilibrium constants, p K − and p K + to define the two conditions in terms of the relative number of charged sites:
The Gran plot is based on the Nernst equation which can be written as = + {+} where E is a measured electrode potential, E 0 is a standard electrode potential, s is the slope, ideally equal to RT/nF, and {H +} is the activity of the hydrogen ion.
The difference between the two measured electromotive force values is proportional to pH. This method of calibration avoids the need to know the standard electrode potential . The proportionality constant, 1/ z , is ideally equal to F R T ln 10 {\displaystyle {\frac {F}{RT\ln {10}}}\ } , the "Nernstian slope".