title: 1H 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 biopolymer environment in solutions through relaxation time 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.
authors.affiliation: INSERM unité 646, Ingénierie de la Vectorisation Particulaire, 10 rue A. Boquel, 49100 Angers, France.
authors.forename: V
authors.initials: V
authors.lastname: Ducel
authors.forename: D
authors.initials: D
authors.lastname: Pouliquen
authors.forename: J
authors.initials: J
authors.lastname: Richard
authors.forename: F
authors.initials: F
authors.lastname: Boury
mesh_terms: D005615:Freezing; D005903:Gliadin / Q000737:chemistry; D006170:Gum Arabic / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D018532:Pisum sativum / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry*; D012996:Solutions; D013696:Temperature; D014908:Triticum / Q000737:chemistry
chemical_list: D010940:Plant Proteins; D012996:Solutions; D006170:Gum Arabic; D005903:Gliadin