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BASys (Bacterial Annotation System) is a tool for automated annotation of bacterial genomic (chromosomal and plasmid) sequences including gene/protein names, GO functions, COG functions, possible paralogues and orthologues, molecular weights, isoelectric points, operon structures, subcellular localization, signal peptides, transmembrane regions ...
In practice, a protein with an excess of basic aminoacids (arginine, lysine and/or histidine) will bear an isoelectric point roughly greater than 7 (basic), while a protein with an excess of acidic aminoacids (aspartic acid and/or glutamic acid) will often have an isoelectric point lower than 7 (acidic).
The three samples are mixed and loaded onto IEF (isoelectric focusing chromatography) for first dimension and the strip is transferred to a SDS PAGE.After the gel electrophoresis, the gel is scanned with the excitation wavelength of each dye one after the other, so each sample can be seen separately (if we scan the gel at the excitation wavelength of the Cy3 dye, we will see in the gel only ...
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 ...
The LOC100287387 protein is formed by a 423 amino acid peptide sequence. The molecular mass is 44.4 kdal, [ 5 ] and the isoelectric point is 10.77. [ 6 ] There is a G-patch domain and a short domain of unknown function within the peptide sequence.
Isoelectric focusing (IEF), also known as electrofocusing, is a technique for separating different 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 function of the ...
The isoelectric point is 6.52. There are no significant positive or negative charge clusters in the protein. There are no significant positive or negative charge clusters in the protein. There is a stretch of 21 0’s from 254-275 and a stretch of 24 0’s from 420-444.1 [ 14 ]
Most protein separations are performed using a "discontinuous" (or DISC) buffer system that significantly enhances the sharpness of the bands within the gel. During electrophoresis in a discontinuous gel system, an ion gradient is formed in the early stage of electrophoresis that causes all of the proteins to focus into a single sharp band.