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Issue 43, 2016
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The temperature dependence of the Hofmeister series: thermodynamic fingerprints of cosolute–protein interactions

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Abstract

The Hofmeister series is a universal homologous series to rank ion-specific effects on biomolecular properties such as protein stability or aggregation propensity. Although this ranking is widely used, outliers and exceptions are discussed controversially and a molecular level understanding is still lacking. Studying the thermal unfolding equilibrium of RNase A, we here show that this ambiguity arises from the oversimplified approach to determine the ion rankings. Instead of measuring salt effects on a single point of the protein folding stability curve (e.g. the melting point Tm), we here consider the salt induced shifts of the entire protein ‘stability curve’ (the temperature dependence of the unfolding free energy change, ΔGu(T)). We found multiple intersections of these curves, pinpointing a widely ignored fact: the Hofmeister cation and anion rankings are temperature dependent. We further developed a novel classification scheme of cosolute effects based on their thermodynamic fingerprints, reaching beyond salt effects to non-electrolytes.

Graphical abstract: The temperature dependence of the Hofmeister series: thermodynamic fingerprints of cosolute–protein interactions

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Publication details

The article was received on 21 Jul 2016, accepted on 22 Aug 2016 and first published on 22 Aug 2016


Article type: Paper
DOI: 10.1039/C6CP05080H
Citation: Phys. Chem. Chem. Phys., 2016,18, 29698-29708
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    The temperature dependence of the Hofmeister series: thermodynamic fingerprints of cosolute–protein interactions

    M. Senske, D. Constantinescu-Aruxandei, M. Havenith, C. Herrmann, H. Weingärtner and S. Ebbinghaus, Phys. Chem. Chem. Phys., 2016, 18, 29698
    DOI: 10.1039/C6CP05080H

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