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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Submitted on : Tuesday, October 22, 2013 - 8:58:15 AM
Last modification on : Wednesday, April 24, 2019 - 5:08:09 PM

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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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