Salts, interfacial water and protein conformation

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

A phenomenological theory of salt-induced Hofmeister phenomena is presented, based on a relation between protein solubility in salt solutions and protein-water interfacial tension. As a generalization of previous treatments, it implies that both kosmotropic salting-out and chaotropic salting-in are manifested via salt-induced changes of the hydrophobic/hydrophilic properties of protein-water interfaces. The theory is applied to describe the salt-dependent free energy profiles of proteins as a function of their water-exposed surface area. On this basis, three classes of protein conformation have been distinguished. The new formalism accounts for the diverse manifestations of salt effects on protein conformation, dynamics and stability, and resolves the puzzle of chaotropes stabilizing certain proteins (and other anomalies). It is also shown that the relation between interfacial tension and protein structural stability is straightforwardly linked to protein conformational fluctuations, providing a keystone for the microscopic interpretation of Hofmeister effects. Implications of the results concerning the use of Hofmeister effects in the experimental study of protein function are discussed.

Original languageEnglish
Pages (from-to)629-633
Number of pages5
JournalBiotechnology and Biotechnological Equipment
Volume22
Issue number1
Publication statusPublished - Feb 2008

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Protein Conformation
Salts
Water
Proteins
Surface Tension
Protein Stability
Solubility

Keywords

  • Conformational fluctuations
  • Hofmeister effects
  • Interfacial energy
  • Water

ASJC Scopus subject areas

  • Biotechnology

Cite this

Salts, interfacial water and protein conformation. / Dér, A.

In: Biotechnology and Biotechnological Equipment, Vol. 22, No. 1, 02.2008, p. 629-633.

Research output: Contribution to journalArticle

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