About: Hofmeister series is a research topic. Over the lifetime, 1179 publications have been published within this topic receiving 52083 citations.
Papers published on a yearly basis
TL;DR: It is demonstrated that bulk water structure is not central to the Hofmeister effect, and models are being developed that depend upon direct ion-macromolecule interactions as well as interactions with water molecules in the first hydration shell of the macromolecules.
TL;DR: Analysis of solvent isotope effects and of the changes in LCST with ion concentration and identity showed multiple mechanisms were at work, and in solutions containing sufficient concentrations of strongly hydrated anions, the phase transition of PNIPAM was directly correlated with the hydration entropy of the anion.
Abstract: Aqueous processes ranging from protein folding and enzyme turnover to colloidal ordering and macromolecular precipitation are sensitive to the nature and concentration of the ions present in solution. Herein, the effect of a series of sodium salts on the lower critical solution temperature (LCST) of poly(N-isopropylacrylamide), PNIPAM, was investigated with a temperature gradient microfluidic device under a dark-field microscope. While the ability of a particular anion to lower the LCST generally followed the Hofmeister series, analysis of solvent isotope effects and of the changes in LCST with ion concentration and identity showed multiple mechanisms were at work. In solutions containing sufficient concentrations of strongly hydrated anions, the phase transition of PNIPAM was directly correlated with the hydration entropy of the anion. On the other hand, weakly hydrated anions were salted-out through surface tension effects and displayed improved hydration by direct ion binding.
TL;DR: Model compound studies in the literature show how Hofmeister ion interactions affect protein stability, and a general model, suitable for analyzing diverse ion-protein interactions, is provided by the two-domain model of Record and co-workers.
TL;DR: In a seminal series of papers, Franz Hofmeister, Professor of Pharmacology at the University of Prague, was the first to study specific ion effects systematically as discussed by the authors, which stands in the scheme of things in importance much as did the work of Mendel to genetics.
Abstract: Specific ion effects are universal in biology, biochemistry, chemistry and chemical engineering. In a seminal series of papers, Franz Hofmeister, Professor of Pharmacology at the University of Prague was the first to study these effects systematically. His work stands in the scheme of things in importance much as did the work of Mendel to genetics. For over a hundred years Hofmeister effects have not been encompassed by theories of solution or colloid chemistry. It is only recently, the subject of this special issue, that some progress has been made. Hofmeister's work is much quoted. But practically no one has ever actually read his papers (originals in archaic German). They are model scientific works for their, and indeed for our time. This article gives translations of two of his most important contributions.
TL;DR: The surface potential difference and surface tension at an air-salt solution interface are used to generate a simple model for how ions affect protein stability and solubility through indirect interactions at the protein-solution interface.
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