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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 pzc is the same as the isoelectric point (iep) if there is no adsorption of other ions than the potential determining H + /OH − at the surface [clarification needed]. [8] This is often the case for pure ("pristine surface") oxides in suspension in water. In the presence of specific adsorption, pzc and isoelectric point generally have ...
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 ...
The isoelectric point is the pH at which a compound - in this case a protein - has no net charge. A protein's isoelectric point or PI can be determined using the pKa of the side chains, if the amino (positive chain) is able to cancel out the carboxyl (negative) chain, the protein would be at its PI.
From a theoretical viewpoint, the zeta potential is the electric potential in the interfacial double layer (DL) at the location of the slipping plane relative to a point in the bulk fluid away from the interface.
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 ...
Isoelectric focusing (IEF), also known as electrofocusing, is a technique for separating different charged molecules by differences in their isoelectric point (pI). [ 1 ] [ 2 ] It is a type of zone electrophoresis usually performed on proteins in a gel that takes advantage of the fact that overall charge on the molecule of interest is a ...
At the isoelectric point (pI), the total charge on the protein is 0 and it will not bind to the matrix. If the pH is above the pI, the protein will have a negative charge and bind to the matrix in an anion exchange column.