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000821016 1001_ $$0P:(DE-HGF)0$$aBanc, A.$$b0$$eCorresponding author
000821016 245__ $$aSmall angle neutron scattering contrast variation reveals heterogeneities of interactions in protein gels
000821016 260__ $$aLondon$$bRoyal Soc. of Chemistry$$c2016
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000821016 520__ $$aWe propose a quantitative approach to probe the spatial heterogeneities of interactions in macromolecular gels, based on a combination of small angle X-ray (SAXS) and neutrons (SANS) scattering. We investigate the structure of model gluten protein gels and show that the gels display radically different SAXS and SANS profiles when the solvent is (at least partially) deuterated. The detailed analysis of the SANS signal as a function of the solvent deuteration demonstrates heterogeneities of sample deuteration at different length scales. The progressive exchange between the protons (H) of the proteins and the deuteriums (D) of the solvent is inhomogeneous and 60 nm large zones that are enriched in H are evidenced. In addition, at low protein concentration, in the sol state, solvent deuteration induces a liquid/liquid phase separation. Complementary biochemical and structure analyses show that the denser protein phase is more protonated and specifically enriched in glutenin, the polymeric fraction of gluten proteins. These findings suggest that the presence of H-rich zones in gluten gels would arise from the preferential interaction of glutenin polymers through a tight network of non-exchangeable intermolecular hydrogen bonds.
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000821016 65017 $$0V:(DE-MLZ)GC-1602-2016$$2V:(DE-HGF)$$aPolymers, Soft Nano Particles and  Proteins$$x0
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000821016 7001_ $$0P:(DE-HGF)0$$aCharbonneau, C.$$b1
000821016 7001_ $$0P:(DE-HGF)0$$aDahesh, M.$$b2
000821016 7001_ $$0P:(DE-Juel1)130507$$aAppavou, M.-S.$$b3$$ufzj
000821016 7001_ $$0P:(DE-Juel1)130647$$aFu, Z.$$b4$$ufzj
000821016 7001_ $$0P:(DE-HGF)0$$aMorel, M.-H.$$b5
000821016 7001_ $$0P:(DE-HGF)0$$aRamos, L.$$b6
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