Folding of a Salivary Intrinsically Disordered Protein upon Binding to Tannins
Folding of a Salivary Intrinsically Disordered Protein upon Binding to Tannins
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DOI：
10.1021/ja200534f
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发表时间：
2011-05-25
影响因子：
15
通讯作者：
Dugourd, Philippe
中科院分区：
文献类型：
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作者：
Canon, Francis;Ballivian, Renaud;Dugourd, Philippe
我们使用离子迁移谱来探索在复杂的混合物中结合到其目标的内在无序蛋白质的构象适应性。我们研究了人类唾液中富含脯氨酸的蛋白IB 5和葡萄酒和茶单宁模型表没食子儿茶素没食子酸酯（EgCG）之间的相互作用。记录了裸IBS和IBS与N = 1-15单宁络合的碰撞截面。数据表明IBS在与EgCG结合后经历未折叠到折叠的结构转变。
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.