title: The effect of counter ions on the conformation of intrinsically disordered proteins studied by size-exclusion chromatography.
abstract: Counter ions are able to change the conformation of intrinsically disordered proteins (IDPs) to a more compact structure via the reduction of electrostatic repulsion. When the extended IDP conformation is transformed into a more ordered one, the value of the Stokes radius should decrease. Size-exclusion chromatography is a simple method for the determination of the Stokes radius, which describes the hydrodynamic properties of protein molecules. In our paper size-exclusion chromatography experiments of Starmaker (a highly acidic IDP), in the presence of various counter ions, are presented as an example of a simple experimental method, which provides valuable information about subtle counter ions-induced conformational changes in IDP.
authors: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
authors: Magdalena
authors: M
authors: Wojtas
authors: Tomasz M
authors: TM
authors: Kapłon
authors: Piotr
authors: P
authors: Dobryszycki
authors: Andrzej
authors: A
authors: Ożyhar
mesh_terms: D002138:Calibration; D002850:Chromatography, Gel / Q000379:methods*; D057446:Hydrodynamics; D007477:Ions / Q000494:pharmacology; D011487:Protein Conformation / Q000187:drug effects; D029961:Zebrafish Proteins / Q000737:chemistry*
chemical_list: D007477:Ions; D029961:Zebrafish Proteins; C478248:stm protein, zebrafish