title: The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences.
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.
authors.affiliation: Department of Medicine, University of Geneva, Switzerland.
authors.forename: B
authors.initials: B
authors.lastname: Bjellqvist
authors.forename: G J
authors.initials: GJ
authors.lastname: Hughes
authors.forename: C
authors.initials: C
authors.lastname: Pasquali
authors.forename: N
authors.initials: N
authors.lastname: Paquet
authors.forename: F
authors.initials: F
authors.lastname: Ravier
authors.forename: J C
authors.initials: JC
authors.lastname: Sanchez
authors.forename: S
authors.initials: S
authors.lastname: Frutiger
authors.forename: D
authors.initials: D
authors.lastname: Hochstrasser
mesh_terms: D000595:Amino Acid Sequence; D003627:Data Interpretation, Statistical; D004566:Electrodes; D006863:Hydrogen-Ion Concentration; D007477:Ions; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D010455:Peptides / Q000032:analysis*; D015203:Reproducibility of Results; D014508:Urea; D014867:Water
chemical_list: D007477:Ions; D010455:Peptides; D014867:Water; D014508:Urea