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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 (2011-2013)
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
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https://hal.archives-ouvertes.fr/hal-00875405
Contributor : Agnès Bussy <>
Submitted on : Tuesday, October 22, 2013 - 8:58:15 AM
Last modification on : Monday, April 20, 2020 - 9:46:03 AM

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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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