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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.
It is different from the isoelectric point (pI) in that pI is the pH value at which the net charge of the molecule, including bound ions is zero. Whereas the isoionic point is at net charge zero in a deionized solution. Thus, the isoelectric and isoionic points are equal when the concentration of charged species is zero.
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 pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The p K a values of an amino acid side chain in solution is typically inferred from the p K a values of model compounds (compounds that are similar to ...
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.
Isoelectric focusing is the first step in two-dimensional gel electrophoresis, in which proteins are first separated by their pI value and then further separated by molecular weight through SDS-PAGE. Isoelectric focusing, on the other hand, is the only step in preparative native PAGE at constant pH. [5]
Backbone-dependent rotamer library for serine.Each plot shows the population of the χ 1 rotamers of serine as a function of the backbone dihedral angles φ and ψ. In biochemistry, a backbone-dependent rotamer library provides the frequencies, mean dihedral angles, and standard deviations of the discrete conformations (known as rotamers) of the amino acid side chains in proteins as a function ...
It was created by modifying three amino acids. Two positively charged arginine molecules were added to the C-terminus of the B-chain, and they shift the isoelectric point from 5.4 to 6.7, making glargine more soluble at a slightly acidic pH and less soluble at a physiological pH.