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@ARTICLE{Heinen:17773,
      author       = {Heinen, M. and Zanini, F. and Roosen-Runge, F. and
                      Fedunová, D. and Zhang, F. and Hennig, M. and Seydel, T.
                      and Schweins, R. and Sztucki, M. and Antalik, M. and
                      Schreiber, F. and Nägele, G.},
      title        = {{V}iscosity and diffusion: crowding and salt effects in
                      protein solutions},
      journal      = {Soft matter},
      volume       = {8},
      number       = {5},
      issn         = {1744-683X},
      address      = {Cambridge},
      publisher    = {Royal Society of Chemistry (RSC)},
      reportid     = {PreJuSER-17773},
      pages        = {1404-1419},
      year         = {2012},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {We report on a joint experimental–theoretical study of
                      collective diffusion in, and static shear viscosity of
                      solutions of bovine serum albumin (BSA) proteins, focusing
                      on the dependence on protein and salt concentration. Data
                      obtained from dynamic light scattering and rheometric
                      measurements are compared to theoretical calculations based
                      on an analytically treatable spheroid model of BSA with
                      isotropic screened Coulomb plus hard-sphere interactions.
                      The only input to the dynamics calculations is the static
                      structure factor obtained from a consistent theoretical fit
                      to a concentration series of small-angle X-ray scattering
                      (SAXS) data. This fit is based on an integral equation
                      scheme that combines high accuracy with low computational
                      cost. All experimentally probed dynamic and static
                      properties are reproduced theoretically with an at least
                      semi-quantitative accuracy. For lower protein concentration
                      and low salinity, both theory and experiment show a maximum
                      in the reduced viscosity, caused by the electrostatic
                      repulsion of proteins. On employing our theoretical and
                      experimental results, the applicability range of a
                      generalized Stokes–Einstein (GSE) relation connecting
                      viscosity, collective diffusion coefficient, and osmotic
                      compressibility, proposed by Kholodenko and Douglas [Phys.
                      Rev. E, 1995, 51, 1081] is examined. Significant violation
                      of the GSE relation is found, both in experimental data and
                      in theoretical models, in concentrated systems at
                      physiological salinity, and under low-salt conditions for
                      arbitrary protein concentrations.},
      cin          = {ICS-3},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-3-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000298990600019},
      doi          = {10.1039/c1sm06242e},
      url          = {https://juser.fz-juelich.de/record/17773},
}