Supplementary Data to








télécharger 6.97 Kb.
titreSupplementary Data to
date de publication19.11.2017
taille6.97 Kb.
typeDocumentos

Supplementary Data to




Conformational changes in p47phox upon activation highlighted by mass spectrometry coupled to Hydrogen/Deuterium exchange and limited proteolysis.
Julien Marcouxa,b,c,d, Petr Manb,c,d,†, Mathieu Castellana,c,d, Corinne Vivèsa,c,d, Eric Forestb,c,d,, Franck Fieschia,c,d
aLaboratoire des Protéines Membranaires, bLaboratoire de Spectrométrie de Masse des Protéines, CEA, DSV, Institut de Biologie Structurale (IBS), 41 rue Jules Horowitz, Grenoble, F-38027, France; cCNRS, UMR 5075, Grenoble, France; dUniversité Joseph Fourier, Grenoble, France.

After 1h digestion with 0.5‰ trypsin, samples were loaded onto a Protein MacroTrap and desalted with 0.03% TFA for 1 min. Peptides were then eluted on a C18 column and separated by a step gradient (5 min at 35% ACN, 10 min at 45% ACN and 2 min at 100% ACN). We basically obtained two chromatographic peaks, first at 12-14 min (45% ACN) and second at 22-24 min (100% ACN). We show here the spectra obtained for both p47phox∆Cter and p47phoxTM-∆Cter, after deconvolution of sum of scans over each chromatographic peak.



Figure 1: Deconvoluted spectra (first peak) after 1h digestion of p47phox∆Cter (top) and p47phoxTM-∆Cter (bottom) with 0.5‰ trypsin.




Figure 2: Deconvoluted spectra (second peak) after 1h digestion of p47phox WT (top) and p47phox TM (bottom) with 0.5‰ trypsin.





 Corresponding authors :

franck.fieschi@ibs.fr Tel: +334 3878 91 77

eric.forest@ibs.fr Tel: +334 38 78 34 03 Fax: +33 4 38 78 54 94

† Present address :

Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i,  CZ-14220 Prague 4, Czech Republic


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