Study of the interactions between a proline-rich protein and a flavan-3-ol by NMR: Residual structures in the natively unfolded protein provides anchorage points for the ligands

被引：0
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作者：
Pascal, Christine [1 ]
Paté, Franck [1 ]
Cheynier, Véronique [1 ]
Delsuc, Marc-André [2 ,3 ,4 ]
机构：
[1] INRA-UMR Sciences Pour l'Oenologie (SPO), 2 place Pierre Viala, Montpellier F34060, France
[2] INSERM, U554, Montpellier F-34090, France
[3] Université de Montpellier 1 et 2, UMR 5048, Centre de Biochimie Structurale, Montpellier F34090, France
[4] IGBMC, Biomolecular NMR Group, UMR7104, Illkirch F-67400, France
来源：
Biopolymers - Peptide Science Section | 2009年 / 91卷 / 09期
关键词：
All Open Access; Green;
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摘要：
52
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页码：745 / 756
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    不详
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    Biopolymers, 2009, 9 (745-756)
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