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@ARTICLE{Dahesh:171843,
      author       = {Dahesh, Mohsen and Banc, Amélie and Duri, Agnès and
                      Morel, Marie-Hélène and Ramos, Laurence},
      title        = {{P}olymeric {A}ssembly of {G}luten {P}roteins in an
                      {A}queous {E}thanol {S}olvent},
      journal      = {The journal of physical chemistry / B},
      volume       = {118},
      number       = {38},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2014-05400},
      pages        = {11065 - 11076},
      year         = {2014},
      abstract     = {The supramolecular organization of wheat gluten proteins is
                      largely unknown due to the intrinsic complexity of this
                      family of proteins and their insolubility in water. We
                      fractionate gluten in a water/ethanol mixture (50/50 v/v)
                      and obtain a protein extract which is depleted in gliadin,
                      the monomeric part of wheat gluten proteins, and enriched in
                      glutenin, the polymeric part of wheat gluten proteins. We
                      investigate the structure of the proteins in the solvent
                      used for extraction over a wide range of concentration, by
                      combining X-ray scattering and multiangle static and dynamic
                      light scattering. Our data show that, in the ethanol/water
                      mixture, the proteins display features characteristic of
                      flexible polymer chains in a good solvent. In the dilute
                      regime, the proteins form very loose structures of
                      characteristic size 150 nm, with an internal dynamics which
                      is quantitatively similar to that of branched polymer coils.
                      In more concentrated regimes, data highlight a hierarchical
                      structure with one characteristic length scale of the order
                      of a few nm, which displays the scaling with concentration
                      expected for a semidilute polymer in good solvent, and a
                      fractal arrangement at a much larger length scale. This
                      structure is strikingly similar to that of polymeric gels,
                      thus providing some factual knowledge to rationalize the
                      viscoelastic properties of wheat gluten proteins and their
                      assemblies.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218},
      pnm          = {54G - JCNS (POF2-54G24)},
      pid          = {G:(DE-HGF)POF2-54G24},
      experiment   = {EXP:(DE-MLZ)KWS3-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000342396000005},
      pubmed       = {pmid:25171192},
      doi          = {10.1021/jp5047134},
      url          = {https://juser.fz-juelich.de/record/171843},
}