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@ARTICLE{Sauter:825197,
      author       = {Sauter, Andrea and Zhang, Fajun and Szekely, Noemi and
                      Pipich, Vitaliy and Sztucki, Michael and Schreiber, Frank},
      title        = {{S}tructural {E}volution of {M}etastable {P}rotein
                      {A}ggregates in the {P}resence of {T}rivalent {S}alt
                      {S}tudied by ({V}){SANS} and {SAXS}},
      journal      = {The journal of physical chemistry / B},
      volume       = {120},
      number       = {24},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2016-07668},
      pages        = {5564 - 5571},
      year         = {2016},
      abstract     = {We present a study of the structural evolution of protein
                      aggregates formed in solutions of a globular protein,
                      β-lactoglobulin (BLG), in the presence of YCl3. These
                      aggregates are often observed before crystallization starts
                      and they are metastable with respect to the crystalline
                      phase. Here we focus on the characterization of the
                      hierarchical structure of this intermediate phase and its
                      temperature dependent structure evolution using a
                      combination of (very) small angle neutron and X-ray
                      scattering (VSANS, SANS, and SAXS). Results show that the
                      hierarchical structure ranges from nanometer scale protein
                      monomer, dimer and compact protein clusters to micrometer
                      scale fractal protein aggregates. Upon cooling, the overall
                      hierarchical structure is preserved, but the evolution of
                      the internal structure within the aggregates is clearly
                      visible: the monomer–monomer correlation peak reduces its
                      intensity and disappears completely at lower temperatures,
                      whereas the cluster–cluster correlation is enhanced. At a
                      larger length scale, the fractal dimension of protein
                      aggregates increases. The kinetics of the structure change
                      during a temperature ramp was further investigated using
                      time-resolved SAXS. The time dependent SAXS profiles show
                      clear isosbestic points and the kinetics of the structural
                      evolution can be well described using a two-state model.
                      These dynamic properties of protein aggregates on a broad
                      length scale may be essential for being the precursors of
                      nucleation.},
      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)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101 / EXP:(DE-MLZ)KWS3-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000378663600024},
      doi          = {10.1021/acs.jpcb.6b03559},
      url          = {https://juser.fz-juelich.de/record/825197},
}