An analysis of the molecular origin of osmolyte-dependent protein stability

Jörg Rösgen, Bernard Pettitt, David Wayne Bolen

Research output: Contribution to journalArticle

73 Citations (Scopus)

Abstract

Protein solvation is the key determinant for isothermal, concentration-dependent effects on protein equilibria, such as folding. The required solvation information can be extracted from experimental thermodynamic data using Kirkwood-Buff theory. Here we derive and discuss general properties of proteins and osmolytes that are pertinent to their biochemical behavior. We find that hydration depends very little on osmolyte concentration and type. Strong dependencies on both osmolyte concentration and type are found for osmolyte self-solvation and protein-osmolyte solvation changes upon unfolding. However, solvation in osmolyte solutions does not involve complex concentration dependencies as found in organic molecules that are not used as osmolytes in nature. It is argued that the simple solvation behavior of naturally occurring osmolytes is a prerequisite for their usefulness in osmotic regulation in vivo. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)733-743
Number of pages11
JournalProtein Science
Volume16
Issue number4
DOIs
StatePublished - Apr 2007
Externally publishedYes

Fingerprint

Protein Stability
Solvation
Proteins
Thermodynamics
Ports and harbors
Hydration
Molecules

Keywords

  • Osmolyte
  • Protein stability
  • Solvation
  • Water structure

ASJC Scopus subject areas

  • Biochemistry

Cite this

An analysis of the molecular origin of osmolyte-dependent protein stability. / Rösgen, Jörg; Pettitt, Bernard; Bolen, David Wayne.

In: Protein Science, Vol. 16, No. 4, 04.2007, p. 733-743.

Research output: Contribution to journalArticle

Rösgen, Jörg ; Pettitt, Bernard ; Bolen, David Wayne. / An analysis of the molecular origin of osmolyte-dependent protein stability. In: Protein Science. 2007 ; Vol. 16, No. 4. pp. 733-743.
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