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Conserved nucleation sites reinforce the significance of Phi value analysis in protein-folding studies

Authors :
Gianni, Stefano
Jemth, P.
Department of Chemistry [Cambridge, UK]
University of Cambridge [UK] (CAM)
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]
Department of Medical Biochemistry and Microbiology
Uppsala University
This work was funded by the Swedish Research Council (to P.J.) and the Italian Ministry of University and Research (PNRCNR Aging Program 2012–2014) (to S.G.) and Sapienza University of Rome (C26A13T9NB to S.G.)
Source :
IUBMB Life, IUBMB Life, Wiley, 2014, 66 (7), pp.449-52. ⟨10.1002/iub.1287⟩
Publication Year :
2014
Publisher :
HAL CCSD, 2014.

Abstract

International audience; The only experimental strategy to address the structure of folding transition states, the so-called Φ value analysis, relies on the synergy between site directed mutagenesis and the measurement of reaction kinetics. Despite its importance, the Φ value analysis has been often criticized and its power to pinpoint structural information has been questioned. In this hypothesis, we demonstrate that comparing the Φ values between proteins not only allows highlighting the robustness of folding pathways but also provides per se a strong validation of the method.

Details

Language :
English
ISSN :
15216543 and 15216551
Database :
OpenAIRE
Journal :
IUBMB Life, IUBMB Life, Wiley, 2014, 66 (7), pp.449-52. ⟨10.1002/iub.1287⟩
Accession number :
edsair.pmid.dedup....79f5d88ff45cb611f1e7bd8260cf84e8