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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.
[72] [73] [74] The isoelectric point of a given molecule is a function of its pK values, so different molecules have different isoelectric points. This permits a technique called isoelectric focusing , [ 75 ] which is used for separation of proteins by 2-D gel polyacrylamide gel electrophoresis .
For each non-linear group, the tables give the most standard notation of the finite group isomorphic to the point group, followed by the order of the group (number of invariant symmetry operations). The finite group notation used is: Z n : cyclic group of order n , D n : dihedral group isomorphic to the symmetry group of an n –sided regular ...
The iso-electric point is the pH value at which the zeta potential is approximately zero. At a pH near the iso-electric point (± 2 pH units), colloids are usually unstable; the particles tend to coagulate or flocculate. Such titrations use acids or bases as titration reagents. Tables of iso-electric points for different materials are available ...
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 two dimensions that proteins are separated into using this technique can be isoelectric point, protein complex mass in the native state, or protein mass. [citation needed] The separation by isoelectric point is called isoelectric focusing. Thereby, a pH gradient is applied to a gel and an electric potential is applied across the gel, making ...
It works on almost any kind of charged molecule—including small inorganic anions, [2] large proteins, [3] small nucleotides, [4] and amino acids. However, ion chromatography must be done in conditions that are one pH unit away from the isoelectric point of a protein. [5] The two types of ion chromatography are anion-exchange and cation-exchange.
The ocean contains a natural buffer system to maintain a pH between 8.1 and 8.3. [11] The oceans buffer system is known as the carbonate buffer system. [ 12 ] The carbonate buffer system is a series of reactions that uses carbonate as a buffer to convert C O 2 {\displaystyle \mathrm {CO_{2}} } into bicarbonate . [ 12 ]