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@ARTICLE{Moreno:808415,
      author       = {Moreno, Angel J. and Lo Verso, Federica and Arbe, Arantxa
                      and Pomposo, José A. and Colmenero, Juan},
      title        = {{C}oncentrated {S}olutions of {S}ingle-{C}hain
                      {N}anoparticles: {A} {S}imple {M}odel for {I}ntrinsically
                      {D}isordered {P}roteins under {C}rowding {C}onditions},
      journal      = {The journal of physical chemistry letters},
      volume       = {7},
      number       = {5},
      issn         = {1948-7185},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2016-02238},
      pages        = {838 - 844},
      year         = {2016},
      abstract     = {By means of large-scale computer simulations and
                      small-angle neutron scattering (SANS), we investigate
                      solutions of single-chain nanoparticles (SCNPs), covering
                      the whole concentration range from infinite dilution to melt
                      density. The analysis of the conformational properties of
                      the SCNPs reveals that these synthetic nano-objects share
                      basic ingredients with intrinsically disordered proteins
                      (IDPs), as topological polydispersity, generally sparse
                      conformations, and locally compact domains. We investigate
                      the role of the architecture of the SCNPs in their collapse
                      behavior under macromolecular crowding. Unlike in the case
                      of linear macromolecules, which experience the usual
                      transition from self-avoiding to Gaussian random-walk
                      conformations, crowding leads to collapsed conformations of
                      SCNPs resembling those of crumpled globules. This behavior
                      is already found at volume fractions (about $30\%)$ that are
                      characteristic of crowding in cellular environments. The
                      simulation results are confirmed by the SANS experiments.
                      Our results for SCNPs—a model system free of specific
                      interactions—propose a general scenario for the effect of
                      steric crowding on IDPs: collapse from sparse conformations
                      at high dilution to crumpled globular conformations in cell
                      environments.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218},
      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},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000371563700019},
      doi          = {10.1021/acs.jpclett.6b00144},
      url          = {https://juser.fz-juelich.de/record/808415},
}