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Ions at Biological Interfaces

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Encyclopedia of Applied Electrochemistry

Historical Overview

The effects of salt ions on the behavior of biomolecules in solutions, such as salting out of proteins, has been traditionally ascribed to ion–water interactions in the aqueous bulk [1]. The ion-specific behavior, expressed, e.g., in the famous Hofmeister series [2, 3], has been then rationalized by classifying ions as either kosmotropes (“structure makers”) or chaotropes (“structure breakers”) according to their ability to structure water molecules around themselves [4]. According to this picture, cosmotropes, but not chaotropes, organize layers of water molecules around themselves, thus effectively removing the solvent from proteins, which leads to salting out. There is, however, mounting experimental evidence that this picture is incomplete at best and that ions (at least monovalent ones) are not able to strongly affect more water molecules than their immediate hydration shells [5–7]. Alternative or additional explanations of salt action are, therefore, being...

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Author information

Authors and Affiliations

  1. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nam. 2, 16610, Prague, Czech Republic

    Pavel Jungwirth

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  1. Pavel Jungwirth
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Correspondence to Pavel Jungwirth .

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Editors and Affiliations

  1. Eppstein, Germany

    Gerhard Kreysa

  2. Yokohama National University, Fac. Engineering, Yokohama, Japan

    Ken-ichiro Ota

  3. Case Western Reserve University, Cleveland, OH, USA

    Robert F. Savinell

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Jungwirth, P. (2014). Ions at Biological Interfaces. In: Kreysa, G., Ota, Ki., Savinell, R.F. (eds) Encyclopedia of Applied Electrochemistry. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-6996-5_441

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