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@ARTICLE{Matsarskaia:868316,
      author       = {Matsarskaia, Olga and Da Vela, Stefano and Mariani,
                      Alessandro and Fu, Zhendong and Zhang, Fajun and Schreiber,
                      Frank},
      title        = {{P}hase-{S}eparation {K}inetics in {P}rotein–{S}alt
                      {M}ixtures with {C}ompositionally {T}uned {I}nteractions},
      journal      = {The journal of physical chemistry / B B, Condensed matter,
                      materials, surfaces, interfaces $\&$ biophysical},
      volume       = {123},
      number       = {9},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2019-06866},
      pages        = {1913 - 1919},
      year         = {2019},
      abstract     = {Liquid–liquid phase separation (LLPS) in protein systems
                      is relevant for many phenomena, from protein condensation
                      diseases to subcellular organization to possible pathways
                      toward protein crystallization. Understanding and
                      controlling LLPS in proteins is therefore highly relevant
                      for various areas of (biological) soft matter research.
                      Solutions of the protein bovine serum albumin (BSA) have
                      been shown to have a lower critical solution
                      temperature–LLPS (LCST–LLPS) induceable by multivalent
                      salts. Importantly, the nature of the multivalent cation
                      used influences the LCST–LLPS in such systems. Here, we
                      present a systematic ultrasmall-angle X-ray scattering
                      investigation of the kinetics of LCST–LLPS of BSA in the
                      presence of different mixtures of HoCl3 and LaCl3, resulting
                      in different effective interprotein attraction strengths. We
                      monitor the characteristic length scales ξ(t, Tfin) after
                      inducing LLPS by subjecting the respective systems to
                      temperature jumps in their liquid–liquid coexistence
                      regions. With increasing interprotein attraction and
                      increasing Tfin, we observe an increasing deviation from the
                      growth law of ξ ∼ t1/3 and an increased trend toward
                      arrest. We thus establish a multidimensional method to tune
                      phase transitions in our systems. Our findings help shed
                      light on general questions regarding LLPS and the tunability
                      of its kinetics in both proteins and colloidal systems.},
      cin          = {JCNS-1 / JCNS-FRM-II / MLZ},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)KWS3-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30702291},
      UT           = {WOS:000460996400004},
      doi          = {10.1021/acs.jpcb.8b10725},
      url          = {https://juser.fz-juelich.de/record/868316},
}