Folding of a salivary intrinsically disordered protein upon binding to tannins

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.
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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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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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