Chemical unfolding of enolase from Saccharomyces cerevisiae exhibits a three-state model.

The Protein Journal
Dénison S Sánchez-MiguelClaudia G Benítez-Cardoza

Abstract

Enolase is a multifunctional protein that participates in glycolysis and gluconeogenesis and can act as a plasminogen receptor on the cell surface of several organisms, among other functions. Despite its participation in a variety of biological and pathophysiological processes, its stability and folding/unfolding reaction have not been fully explored. In this paper we present, the urea and GdnHCl-induced denaturation of enolase studied by means of fluorescence and circular dichroism spectroscopies. We found that enolase unfolds through a highly reversible pathway, populating a stable intermediate species in a range of experimental conditions. The refolding reaction also exhibits an intermediate state that might have a slightly more compact conformation compared to the unfolding intermediate. The thermodynamic parameters associated with the unfolding reaction are presented and discussed.

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Citations

Jan 31, 2012·International Journal of Biological Macromolecules·Tzu-Ting ChuangLong-Liu Lin
Sep 7, 2011·International Journal of Biological Macromolecules·Liliana M Moreno-VargasClaudia G Benítez-Cardoza
Jan 31, 2012·Archives of Biochemistry and Biophysics·Francisco Adriano O CarvalhoMarcel Tabak
Nov 1, 2011·Biochemistry·Anbazhagan VeerappanDirk Schneider
Jan 17, 2019·BioMed Research International·María de J López-LópezXianwu Guo

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