The kinetics of folding of frataxin
| Autor: | Annalisa Pastore, Angelo Toto, Angela Morrone, Stefano Gianni, Daniela Bonetti, Rajanish Giri, Maurizio Brunori, Pierandrea Temussi, Domenico Sanfelice |
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| Přispěvatelé: | Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Università degli Studi di Roma 'La Sapienza' [Rome], Institut Pasteur - Fondation Cenci Bolognetti, Réseau International des Instituts Pasteur - Institut Pasteur - Fondation Cenci Bolognetti, Division of Molecular Structure, National Institute for Medical Research (MRC), Department of Neuroscience, Wohl Institute, Dipartimento di Chimica, Università degli studi di Napoli Federico II [Napoli], Department of Chemistry (Cambridge, UK), University of Cambridge (UK), This work was partly supported by grants from the Italian Ministero dell'Istruzione dell'Universita e dellaRicerca (Progretto di Interesse 'Invecchiamento' to S.G.), Sapienza University of Rome (C26A13T9NB to S.G.) and EMBO (to S.G.), Department of Biochemical Sciences 'Rossi Fanelli', Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Réseau International des Instituts Pasteur (RIIP), Università degli studi di Napoli Federico II, Department of Chemistry [Cambridge, UK], University of Cambridge [UK] (CAM), Bonetti, Daniela, Toto, Angelo, Giri, Rajanish, Morrone, Angela, Sanfelice, Domenico, Pastore, Annalisa, Temussi, Pierandrea, Gianni, Stefano, Brunori, Maurizio |
| Rok vydání: | 2014 |
| Předmět: |
Protein Structure
MESH: Hydrogen-Ion Concentration General Physics and Astronomy Phi value analysis Settore BIO/11 - Biologia Molecolare Saccharomyces cerevisiae MESH: Recombinant Proteins Physics and Astronomy (all) MESH: Protein Structure Tertiary Protein structure Thermodynamic Iron-Binding Proteins [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology Urea Denaturation (biochemistry) [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Iron-Binding Protein Physical and Theoretical Chemistry MESH: Iron-Binding Proteins MESH: Urea Protein Unfolding Kinetic biology MESH: Kinetics Chemistry Temperature Recombinant Protein Hydrogen-Ion Concentration MESH: Saccharomyces cerevisiae Molten globule MESH: Temperature Recombinant Proteins Protein Structure Tertiary Folding (chemistry) Kinetics Biochemistry MESH: Protein Unfolding Frataxin biology.protein Unfolded protein response Thermodynamics Protein folding MESH: Thermodynamics Tertiary |
| Zdroj: | Physical Chemistry Chemical Physics Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2014, 16 (14), pp.6391-7. <10.1039/c3cp54055c> Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2014, 16 (14), pp.6391-7. ⟨10.1039/c3cp54055c⟩ |
| ISSN: | 1463-9084 1463-9076 |
| Popis: | 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. © 2014 the Partner Organisations. |
| Databáze: | OpenAIRE |
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