Folding of a salivary intrinsically disordered protein upon binding to tannins

Francis Canon 1 Renaud Ballivian 1 Fabien Chirot 2 Rodolphe Antoine 3 Pascale Sarni-Manchado 1 Jérôme Lemoine 2 Philippe Dugourd 3
1 SPO - Sciences Pour l'Oenologie
2 ANABIO - ANAlyse BIOmoléculaire RMN et spectrométrie de masse
ISA - Institut des Sciences Analytiques
3 Spectrobio
LASIM - Laboratoire de Spectrométrie Ionique et Moléculaire
Abstract : We used ion mobility spectrometry to explore conformational adaptability of intrinsically disordered proteins bound to their targets in complex mixtures. We investigated the interactions between a human salivary proline-rich protein IB5 and a model of wine and tea tannin: epigallocatechin gallate (EgCG). Collisional cross sections of naked IBS and IBS complexed with N = 1-15 tannins were recorded. The data demonstrate that IBS undergoes an unfolded to folded structural transition upon binding with EgCG.
Keywords : EXCHANGE MOLECULAR-DYNAMICS ION MOBILITY MEASUREMENTS ANGLE X-RAY GAS-PHASE UNSTRUCTURED PROTEINS MASS-SPECTROMETRY CONFORMATIONS SCATTERING OLIGOMERIZATION CHROMATOGRAPHY
Type de document :
Article dans une revue
Journal of the American Chemical Society, American Chemical Society, 2011, 133 (20), pp.7847-7852. 〈10.1021/ja200534f〉
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https://hal.archives-ouvertes.fr/hal-00875405
Contributeur : Agnès Bussy <>
Soumis le : mardi 22 octobre 2013 - 08:58:15
Dernière modification le : lundi 2 juillet 2018 - 15:07:10

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ISA | LASIM | ENS-LYON | INRA | INC-CNRS | BA | UNIV-MONTPELLIER | UNIV-LYON1 | SPO

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Francis Canon, Renaud Ballivian, Fabien Chirot, Rodolphe Antoine, Pascale Sarni-Manchado, et al.. Folding of a salivary intrinsically disordered protein upon binding to tannins. Journal of the American Chemical Society, American Chemical Society, 2011, 133 (20), pp.7847-7852. 〈10.1021/ja200534f〉. 〈hal-00875405〉

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