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Beyond the Hofmeister Series : Ion-Specific Effects on Proteins and Their Biological Functions

Okur, Halil I.; Hladílková, Jana LU ; Rembert, Kelvin B.; Cho, Younhee; Heyda, Jan; Dzubiella, Joachim; Cremer, Paul S. and Jungwirth, Pavel (2017) In Journal of Physical Chemistry B 121(9). p.1997-2014
Abstract

Ions differ in their ability to salt out proteins from solution as expressed in the lyotropic or Hofmeister series of cations and anions. Since its first formulation in 1888, this series has been invoked in a plethora of effects, going beyond the original salting out/salting in idea to include enzyme activities and the crystallization of proteins, as well as to processes not involving proteins like ion exchange, the surface tension of electrolytes, or bubble coalescence. Although it has been clear that the Hofmeister series is intimately connected to ion hydration in homogeneous and heterogeneous environments and to ion pairing, its molecular origin has not been fully understood. This situation could have been summarized as follows:... (More)

Ions differ in their ability to salt out proteins from solution as expressed in the lyotropic or Hofmeister series of cations and anions. Since its first formulation in 1888, this series has been invoked in a plethora of effects, going beyond the original salting out/salting in idea to include enzyme activities and the crystallization of proteins, as well as to processes not involving proteins like ion exchange, the surface tension of electrolytes, or bubble coalescence. Although it has been clear that the Hofmeister series is intimately connected to ion hydration in homogeneous and heterogeneous environments and to ion pairing, its molecular origin has not been fully understood. This situation could have been summarized as follows: Many chemists used the Hofmeister series as a mantra to put a label on ion-specific behavior in various environments, rather than to reach a molecular level understanding and, consequently, an ability to predict a particular effect of a given salt ion on proteins in solutions. In this Feature Article we show that the cationic and anionic Hofmeister series can now be rationalized primarily in terms of specific interactions of salt ions with the backbone and charged side chain groups at the protein surface in solution. At the same time, we demonstrate the limitations of separating Hofmeister effects into independent cationic and anionic contributions due to the electroneutrality condition, as well as specific ion pairing, leading to interactions of ions of opposite polarity. Finally, we outline the route beyond Hofmeister chemistry in the direction of understanding specific roles of ions in various biological functionalities, where generic Hofmeister-type interactions can be complemented or even overruled by particular steric arrangements in various ion binding sites. (Chemical Equation Presented).

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Physical Chemistry B
volume
121
issue
9
pages
18 pages
publisher
The American Chemical Society
external identifiers
  • scopus:85015895363
  • wos:000396296000001
ISSN
1520-6106
DOI
10.1021/acs.jpcb.6b10797
language
English
LU publication?
yes
id
c9a236d8-3e16-49b2-a6d5-93c1367bd4c9
date added to LUP
2017-04-05 14:38:58
date last changed
2018-10-14 04:38:29
@article{c9a236d8-3e16-49b2-a6d5-93c1367bd4c9,
  abstract     = {<p>Ions differ in their ability to salt out proteins from solution as expressed in the lyotropic or Hofmeister series of cations and anions. Since its first formulation in 1888, this series has been invoked in a plethora of effects, going beyond the original salting out/salting in idea to include enzyme activities and the crystallization of proteins, as well as to processes not involving proteins like ion exchange, the surface tension of electrolytes, or bubble coalescence. Although it has been clear that the Hofmeister series is intimately connected to ion hydration in homogeneous and heterogeneous environments and to ion pairing, its molecular origin has not been fully understood. This situation could have been summarized as follows: Many chemists used the Hofmeister series as a mantra to put a label on ion-specific behavior in various environments, rather than to reach a molecular level understanding and, consequently, an ability to predict a particular effect of a given salt ion on proteins in solutions. In this Feature Article we show that the cationic and anionic Hofmeister series can now be rationalized primarily in terms of specific interactions of salt ions with the backbone and charged side chain groups at the protein surface in solution. At the same time, we demonstrate the limitations of separating Hofmeister effects into independent cationic and anionic contributions due to the electroneutrality condition, as well as specific ion pairing, leading to interactions of ions of opposite polarity. Finally, we outline the route beyond Hofmeister chemistry in the direction of understanding specific roles of ions in various biological functionalities, where generic Hofmeister-type interactions can be complemented or even overruled by particular steric arrangements in various ion binding sites. (Chemical Equation Presented).</p>},
  author       = {Okur, Halil I. and Hladílková, Jana and Rembert, Kelvin B. and Cho, Younhee and Heyda, Jan and Dzubiella, Joachim and Cremer, Paul S. and Jungwirth, Pavel},
  issn         = {1520-6106},
  language     = {eng},
  month        = {03},
  number       = {9},
  pages        = {1997--2014},
  publisher    = {The American Chemical Society},
  series       = {Journal of Physical Chemistry B},
  title        = {Beyond the Hofmeister Series : Ion-Specific Effects on Proteins and Their Biological Functions},
  url          = {http://dx.doi.org/10.1021/acs.jpcb.6b10797},
  volume       = {121},
  year         = {2017},
}