The interfacial tension concept, as revealed by fluctuations

Zoltán Násztor, F. Bogár, A. Dér

Research output: Contribution to journalReview article

5 Citations (Scopus)


A simple, didactic model that could have conclusively interpreted the complexity of specific salt (Hofmeister-) effects on protein solubility and function, using a single physical quantity as a central parameter, has long been missing. Via surveying a row of recent papers we show in this review that a phenomenological formalism based on the salt-induced change of protein-water interfacial tension (Δγ) is able to account for a wide range of Hofmeister effects, including also such "exceptions", where inverse or "V-shaped" Hofmeister series occurs. A close relationship between protein-water interfacial tension and conformational fluctuations is pinpointed on theoretical grounds, then it is shown how one can use a complex experimental arsenal to demonstrate conformational fluctuations on two prototypical proteins, the membrane protein bacteriorhodopsin and the cytoplasmic protein myoglobin. Finally, via the results of recent and new molecular dynamics simulations on a model peptide, the tryptophan-cage miniprotein, independent evidences are given in favor of the interfacial tension concept, at the same time demonstrating the predictive power of the theory. It is shown that salt-induced fluctuation changes of surface-exposed amino acid groups can be used as a sensitive measure for mapping the local features of Hofmeister effects on protein conformations. General implications of the interfacial tension concept are also discussed.

Original languageEnglish
Pages (from-to)29-40
Number of pages12
JournalCurrent Opinion in Colloid and Interface Science
Publication statusPublished - Jun 1 2016


  • Conformational fluctuations
  • Hofmeister effects
  • Protein-water interfacial tension

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Polymers and Plastics
  • Colloid and Surface Chemistry
  • Surfaces and Interfaces

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