FAO AGRIS - International System for Agricultural Science and Technology

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.

2009

Pascal, Christine | Paté, Franck | Cheynier, Véronique | Delsuc, Marc-André | Sciences Pour l'Oenologie (SPO) ; Université Montpellier 1 (UM1)-Institut National de la Recherche Agronomique (INRA)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro) | Centre de Biochimie Structurale [Montpellier] (CBS) ; Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS) | Institut de génétique et biologie moléculaire et cellulaire (IGBMC) ; Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)


Bibliographic information
Publisher
CCSD, Wiley
Other Subjects
Salivary proline-rich proteins; Molecular sequence data; Protein conformation; Amino acid sequence; Protein folding; Biomolecular; [sdv]life sciences [q-bio]; Nuclear magnetic resonance
Language
English
ISBN
0002683428000
ISSN
00420163, 19402144
Type
Journal Article; Journal Part; Journal Article; Journal Part
Source
ISSN: 0006-3525, EISSN: 1097-0282, Biopolymers, https://inserm.hal.science/inserm-00420163, Biopolymers, 2009, 91 (9), pp.745-56. ⟨10.1002/bip.21221⟩

2025-06-17
2025-10-24
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