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The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences
Electrophoresis · 1993 · Vol. 14(1) · pp. 1023–1031
Bengt Bjellqvist✉(University of Geneva)Graham J. Hughes(University of Geneva)Christian Pasquali(University of Geneva)Nicole Paquet(University of Geneva)Florence Ravier(University of Geneva)Jean‐Charles Sanchez(University of Geneva)Séverine Frutiger(University of Geneva)Denis F. Hochstrasser(University of Geneva)
Abstract
The focusing positions in narrow range immobilized pH gradients of 29 polypeptides of known amino acid sequence were determined under denaturing conditions. The isoelectric points of the proteins calculated from their amino acid sequences matched with good accuracy the experimentally determined pI values. We show the advantages of being able to predict the position of a protein of known structure within a two-dimensional gel.
Advanced Proteomics Techniques and ApplicationsRNA and protein synthesis mechanismsGlycosylation and Glycoproteins ResearchIsoelectric focusingImmobilized pH gradientIsoelectric pointAmino acidChromatographyChemistryAmino acid residuePeptide sequenceBiochemistryEnzyme
MeSH terms
Amino Acid SequenceData Interpretation, StatisticalElectrodesHydrogen-Ion ConcentrationIonsIsoelectric FocusingIsoelectric PointPeptidesUreaWaterReproducibility of Results
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References
Two‐dimensional electrophoresis. The current state of two‐dimensional electrophoresis with immobilized pH gradients
Electrophoresis · 1988 · 777 citations
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