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@ARTICLE{Boire:858884,
      author       = {Boire, Adeline and Sanchez, Christian and Morel,
                      Marie-Hélène and Lettinga, M.P. and Menut, Paul},
      title        = {{D}ynamics of liquid-liquid phase separation of wheat
                      gliadins},
      journal      = {Scientific reports},
      volume       = {8},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2018-07720},
      pages        = {14441},
      year         = {2018},
      abstract     = {During wheat seeds development, storage proteins are
                      synthetized and subsequently form dense protein phases, also
                      called Protein Bodies (PBs). The mechanisms of PBs formation
                      and the supramolecular assembly of storage proteins in PBs
                      remain unclear. In particular, there is an apparent
                      contradiction between the low solubility in water of storage
                      proteins and their high local dynamics in dense PBs. Here,
                      we probe the interplay between short-range attraction and
                      long-range repulsion of a wheat gliadin isolate by
                      investigating the dynamics of liquid-liquid phase separation
                      after temperature quench. We do so using time-resolved small
                      angle light scattering, phase contrast microscopy and
                      rheology. We show that gliadins undergo liquid-liquid phase
                      separation through Nucleation and Growth or Spinodal
                      Decomposition depending on the quench depth. They assemble
                      into dense phases but remain in a liquid-like state over an
                      extended range of temperatures and concentrations. The
                      analysis of phase separation kinetics reveals that the
                      attraction strength of gliadins is in the same order of
                      magnitude as other proteins. We discuss the respective role
                      of competing interactions, protein intrinsic disorder,
                      hydration and polydispersity in promoting local dynamics and
                      providing this liquid-like behavior despite attractive
                      forces.},
      cin          = {ICS-3},
      ddc          = {600},
      cid          = {I:(DE-Juel1)ICS-3-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30262869},
      UT           = {WOS:000445815700003},
      doi          = {10.1038/s41598-018-32278-5},
      url          = {https://juser.fz-juelich.de/record/858884},
}