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Article dans une revue

(1)H NMR relaxation studies of protein-polysaccharide mixtures

Abstract :

NMR water proton relaxation was used to characterize the structure of plant proteins and plant protein-polysaccharide mixtures in aqueous solutions. The method is based on the mobility determination of the water molecules in the biopolymers environment in solutions through relaxation times measurements. Differences of conformation between pea globulin and alpha gliadin seem to control the water molecules mobility in their environment. As deduced from the study of complexes, the electrostatic interactions may also play a major role in the water molecule motions. The phase separation induced under specific conditions seems to promote the translational diffusion of structured water molecules whereas the rotational motion was more restricted.

Type de document :
Article dans une revue
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https://hal.univ-angers.fr/hal-03171795
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Soumis le : mercredi 17 mars 2021 - 11:12:42
Dernière modification le : jeudi 18 mars 2021 - 03:27:09

Identifiants

  • HAL Id : hal-03171795, version 1
  • OKINA : ua3774

Citation

V. Ducel, Daniel Pouliquen, Jean-Christophe Richard, Frank Boury. (1)H NMR relaxation studies of protein-polysaccharide mixtures. International Journal of Biological Macromolecules, Elsevier, 2008, 43 (4), pp.2616-23. ⟨hal-03171795⟩

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