The kinetics of folding of frataxin. - RIIP - Réseau International des Instituts Pasteur Access content directly
Journal Articles Physical Chemistry Chemical Physics Year : 2014

The kinetics of folding of frataxin.


The role of the denatured state in protein folding represents a key issue for the proper evaluation of folding kinetics and mechanisms. The yeast ortholog of the human frataxin, a mitochondrial protein essential for iron homeostasis and responsible for Friedreich's ataxia, has been shown to undergo cold denaturation above 0 °C, in the absence of chemical denaturants. This interesting property provides the unique opportunity to explore experimentally the molecular mechanism of both the hot and cold denaturation. In this work, we present the characterization of the temperature and urea dependence of the folding kinetics of yeast frataxin, and show that while at neutral pH and in the absence of a denaturant a simple two-state model may satisfactorily describe the temperature dependence of the folding and unfolding rate constants, the results obtained in urea over a wide range of pH reveal an intriguing complexity, suggesting that folding of frataxin involves a broad smooth free energy barrier.
Embargoed file
Embargoed file
Visibility date is undetermined

Dates and versions

pasteur-01181218 , version 1 (29-07-2015)



Daniela Bonetti, Angelo Toto, Rajanish Giri, Angela Morrone, Domenico Sanfelice, et al.. The kinetics of folding of frataxin.. Physical Chemistry Chemical Physics, 2014, 16 (14), pp.6391-7. ⟨10.1039/c3cp54055c⟩. ⟨pasteur-01181218⟩


52 View
3 Download



Gmail Facebook X LinkedIn More