title: 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 IB5 and IB5 complexed with N = 1-15 tannins were recorded. The data demonstrate that IB5 undergoes an unfolded to folded structural transition upon binding with EgCG.
authors.affiliation: INRA, UMR1083 Science Pour l'Oenologie, Polyphenol Interaction, Bât 28, 2 place Viala F-34060 Montpellier, France.
authors.forename: Francis
authors.initials: F
authors.lastname: Canon
authors.forename: Renaud
authors.initials: R
authors.lastname: Ballivian
authors.forename: Fabien
authors.initials: F
authors.lastname: Chirot
authors.forename: Rodolphe
authors.initials: R
authors.lastname: Antoine
authors.forename: Pascale
authors.initials: P
authors.lastname: Sarni-Manchado
authors.forename: Jérôme
authors.initials: J
authors.lastname: Lemoine
authors.forename: Philippe
authors.initials: P
authors.lastname: Dugourd
mesh_terms: D002942:Circular Dichroism; D013058:Mass Spectrometry / Q000379:methods; D011485:Protein Binding; D017510:Protein Folding; D012471:Salivary Proteins and Peptides / Q000378:metabolism*; D013634:Tannins / Q000378:metabolism*
chemical_list: D012471:Salivary Proteins and Peptides; D013634:Tannins