Skip to Main content Skip to Navigation
Journal articles

The kinetics of folding of frataxin.

Abstract : 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.
Document type :
Journal articles
Complete list of metadatas

Cited literature [32 references]  Display  Hide  Download

https://hal-riip.archives-ouvertes.fr/pasteur-01181218
Contributor : Istituto Pasteur Fondazione Cenci Bolognetti <>
Submitted on : Wednesday, July 29, 2015 - 2:59:25 PM
Last modification on : Wednesday, October 28, 2020 - 3:20:08 PM
Long-term archiving on: : Friday, October 30, 2015 - 10:25:47 AM

File

 Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed until : jamais

Please log in to resquest access to the document

Identifiers

Collections

Citation

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

Share

Metrics

Record views

162