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.
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Acknowledgment
This work was financed by the National Science Centre grant N N204 120040 (to P.D.) and by a statutory activity subsidy from the Polish Ministry of Science and Higher Education for the Faculty of Chemistry of Wrocław University of Technology.
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Wojtas, M., Kapłon, T.M., Dobryszycki, P., Ożyhar, A. (2012). The Effect of Counter Ions on the Conformation of Intrinsically Disordered Proteins Studied by Size-Exclusion Chromatography. In: Uversky, V., Dunker, A. (eds) Intrinsically Disordered Protein Analysis. Methods in Molecular Biology, vol 896. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-3704-8_21
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DOI: https://doi.org/10.1007/978-1-4614-3704-8_21
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