Folding of a Salivary Intrinsically Disordered Protein upon Binding to Tannins

Folding of a Salivary Intrinsically Disordered Protein upon Binding to Tannins

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 (E...

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Veröffentlicht in:Journal of the American Chemical Society 2011-05, Vol.133 (20), p.7847-7852
Hauptverfasser: Canon, Francis, Ballivian, Renaud, Chirot, Fabien, Antoine, Rodolphe, Sarni-Manchado, Pascale, Lemoine, Jérôme, Dugourd, Philippe
Format: Artikel
Sprache:eng
Schlagworte:
Analytical chemistry
Chemical Sciences
Circular Dichroism
Mass Spectrometry - methods
or physical chemistry
Protein Binding
Protein Folding
Salivary Proteins and Peptides - metabolism
Tannins - metabolism
Theoretical and
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Beschreibung
Zusammenfassung: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.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja200534f