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@ARTICLE{Banc:821016,
      author       = {Banc, A. and Charbonneau, C. and Dahesh, M. and Appavou,
                      M.-S. and Fu, Z. and Morel, M.-H. and Ramos, L.},
      title        = {{S}mall angle neutron scattering contrast variation reveals
                      heterogeneities of interactions in protein gels},
      journal      = {Soft matter},
      volume       = {12},
      number       = {24},
      issn         = {1744-6848},
      address      = {London},
      publisher    = {Royal Soc. of Chemistry},
      reportid     = {FZJ-2016-06273},
      pages        = {5340 - 5352},
      year         = {2016},
      abstract     = {We 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.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623) / NMI3-II - Neutron
                      Scattering and Muon Spectroscopy Integrated Initiative
                      (283883)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4 /
                      G:(EU-Grant)283883},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101 / EXP:(DE-MLZ)KWS3-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000378934400011},
      pubmed       = {pmid:27198847},
      doi          = {10.1039/C6SM00710D},
      url          = {https://juser.fz-juelich.de/record/821016},
}