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Why pH titration in protein solutions follows a Hofmeister series
Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Theoretical Physics .
University of Florence.
University of Florence.
University of Florence.
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2006 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, Vol. 110, no 14, 7563-7566 p.Article in journal (Refereed) Published
Abstract [en]

Measurements of pH in single-phase cytochrome c suspensions are reported. The pH, as determined by a glass electrode, has a fixed value. With the addition of salt, the supposedly fixed pH changes strongly. The pH depends on salt type and concentration and follows a Hofmeister series. A theoretical interpretation is given that provides insights into such Hofmeister effects. These occur generally in protein solutions. While classical electrostatic models provide partial understanding of such trends in protein solutions, they fail to explain the observed ion specificity. Such models neglect electrodynamic fluctuation (dispersion) forces acting between ions and proteins. We use a Poisson-Boltzmann cell model that takes these ionic dispersion potentials between ions and proteins into account. The observed ion specificity can then be accounted for. Proteins act as buffers that display similar salt-dependent pH trends not previously explained.

Place, publisher, year, edition, pages
2006. Vol. 110, no 14, 7563-7566 p.
National Category
Natural Sciences
URN: urn:nbn:se:liu:diva-33853DOI: 10.1021/jp051025tLocal ID: 19926OAI: diva2:254676
Available from: 2009-10-09 Created: 2009-10-09 Last updated: 2011-01-11

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Boström, Mathias
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The Institute of TechnologyTheoretical Physics
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