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The isoelectric point (pI, pH(I), IEP), is the pH at which a molecule carries no net electrical charge or is electrically neutral in the statistical mean. The standard nomenclature to represent the isoelectric point is pH(I). [1] However, pI is also used. [2] For brevity, this article uses pI.
The pI of most proteins is in the pH range of 4–6. Mineral acids, such as hydrochloric and sulfuric acid are used as precipitants. The greatest disadvantage to isoelectric point precipitation is the irreversible denaturation caused by the mineral acids.
The pH range is commonly given as zero to 14, but a pH value can be less than 0 for very concentrated strong acids or greater than 14 for very concentrated strong bases. [2] The pH scale is traceable to a set of standard solutions whose pH is established by international agreement. [3]
The pH scale is by far the most commonly used acidity function, and is ideal for dilute aqueous solutions. Other acidity functions have been proposed for different environments, most notably the Hammett acidity function , H 0 , [ 3 ] for superacid media and its modified version H − for superbasic media.
The digits of pi extend into infinity, and pi is itself an irrational number, meaning it can’t be truly represented by an integer fraction (the one we often learn in school, 22/7, is not very ...
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).
The pH-dependent effects cannot be added in the same straightforward way and have to be accounted for using Boltzmann summation, Tanford–Roxby iterations or other methods. The interplay of the intrinsic p K a values of a system with the electrostatic interaction energies between titratable groups can produce quite spectacular effects such as ...
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