Protein folding, stability, and solvation structure in osmolyte solutions

Jörg Rösgen, Bernard Pettitt, David Wayne Bolen

Research output: Contribution to journalArticle

113 Citations (Scopus)

Abstract

An understanding of the impact of the crowded conditions in the cytoplasm on its biomolecules is of clear importance to biochemical, medical, and pharmaceutical science. Our previous work on the use of small biochemical compounds to crowd protein solutions indicates that a quantitative description of their nonideal behavior is possible and straightforward. Here, we show the structural origin of the nonideal solution behavior. We discuss the consequences of these findings regarding protein folding stability and solvation in crowded solutions through a structural analysis of the m-value or the change in free-energy difference of a macromolecule in solution with respect to the concentration of a third component.

Original languageEnglish (US)
Pages (from-to)2988-2997
Number of pages10
JournalBiophysical Journal
Volume89
Issue number5
DOIs
StatePublished - Nov 2005
Externally publishedYes

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Protein Stability
Protein Folding
Cytoplasm
Pharmaceutical Preparations
Proteins

ASJC Scopus subject areas

  • Biophysics

Cite this

Protein folding, stability, and solvation structure in osmolyte solutions. / Rösgen, Jörg; Pettitt, Bernard; Bolen, David Wayne.

In: Biophysical Journal, Vol. 89, No. 5, 11.2005, p. 2988-2997.

Research output: Contribution to journalArticle

Rösgen, Jörg ; Pettitt, Bernard ; Bolen, David Wayne. / Protein folding, stability, and solvation structure in osmolyte solutions. In: Biophysical Journal. 2005 ; Vol. 89, No. 5. pp. 2988-2997.
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