Folding of a Salivary Intrinsically Disordered Protein upon Binding to Tannins

作者：Francis Canon, Renaud Ballivian, Fabien Chirot, Rodolphe Antoine, Pascale Sarni‐Manchado, Jerome L. Lemoine, Philippe Dugourd · 发表于：Journal of the American Chemical Society · 年份：2011 · DOI：10.1021/ja200534f · 被引用次数：91 · 研究领域：Mass Spectrometry Techniques and Applications、Muscle metabolism and nutrition、Fermentation and Sensory Analysis

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.