Folding of a salivary intrinsically disordered protein upon binding to tannins

Francis Canon; Renaud Ballivian; Fabien Chirot; Rodolphe Antoine; Pascale Sarni-Manchado; Jérôme Lemoine; Philippe Dugourd

doi:10.1021/ja200534f

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

Document type :

Journal articles

Domain :

Chemical Sciences / Theoretical and/or physical chemistry

Chemical Sciences / Analytical chemistry

Liste complète des métadonnées

https://hal.archives-ouvertes.fr/hal-00875405
Contributor : Agnès Bussy <>
Submitted on : Tuesday, October 22, 2013 - 8:58:15 AM
Last modification on : Wednesday, April 24, 2019 - 5:08:09 PM

Folding of a salivary intrinsically disordered protein upon binding to tannins

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Folding of a salivary intrinsically disordered protein upon binding to tannins

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