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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 LRRN3 protein is 708 amino acids in length. The molecular weight of this protein is 79,424 daltons, with an isoelectric point of 8.02. [9] It is known to be a single-pass type I membrane protein because it spans the membrane once, with its N-terminus on the extracellular side of the membrane, and its signal sequence is removed.
The isoelectric point (pI) is the pH of a solution at which the net primary charge of a protein becomes zero. At a solution pH that is above the pI the surface of the protein is predominantly negatively charged and therefore like-charged molecules will exhibit repulsive forces.
where c = composition, p = polarity, and v = molecular volume; and are constants of squares of the inverses of the mean distance for each property, respectively equal to 1.833, 0.1018, 0.000399. According to Grantham's distance, most similar amino acids are leucine and isoleucine and the most distant are cysteine and tryptophan.
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.
The isoionic point is the pH value at which a zwitterion molecule has an equal number of positive and negative charges and no adherent ionic species. It was first defined by S.P.L. Sørensen , Kaj Ulrik Linderstrøm-Lang and Ellen Lund in 1926 [ 1 ] and is mainly a term used in protein sciences.
It has a predicted MW of 17.8 kDa and isoelectric point of 5.7 pI. [9] LSMEM2 is predicted to have one transmembrane region which is composed of 50% leucine and considered leucine rich. [10] The N-terminus is predicted to be the cytosolic/intracellular region of the protein, while the C-terminus is predicted as the lumenal/extracellular region ...
Hen egg white lysozyme is thermally stable, with a melting point reaching up to 72 °C at pH 5.0. [5] However, lysozyme in human milk loses activity very quickly at that temperature. [6] Hen egg white lysozyme maintains its activity in a large range of pH (6–9). [7] Its isoelectric point is 11.35. [8]