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Article Dans Une Revue Journal of the American Chemical Society Année : 2011

Folding of a salivary intrinsically disordered protein upon binding to tannins

Francis Canon
Rodolphe Antoine
Pascale Manchado-Sarni
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Philippe Dugourd

Résumé

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.
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Dates et versions

hal-00875405 , version 1 (22-10-2013)

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