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@ARTICLE{Riest:862616,
      author       = {Riest, Jonas and Naegele, Gerhard and Liu, Yun and Wagner,
                      Norman J. and Godfrin, P. Douglas},
      title        = {{S}hort-time dynamics of lysozyme solutions with competing
                      short-range attraction and long-range repulsion:
                      {E}xperiment and theory},
      journal      = {The journal of chemical physics},
      volume       = {148},
      number       = {6},
      issn         = {1089-7690},
      address      = {Melville, NY},
      publisher    = {American Institute of Physics},
      reportid     = {FZJ-2019-02885},
      pages        = {065101 -},
      year         = {2018},
      abstract     = {Recently, atypical static features of microstructural
                      ordering in low-salinity lysozyme protein solutions have
                      been extensively explored experimentally and explained
                      theoretically based on a short-range attractive plus
                      long-range repulsive (SALR) interaction potential. However,
                      the protein dynamics and the relationship to the atypical
                      SALR structure remain to be demonstrated. Here, the
                      applicability of semi-analytic theoretical methods
                      predicting diffusion properties and viscosity in isotropic
                      particle suspensions to low-salinity lysozyme protein
                      solutions is tested. Using the interaction potential
                      parameters previously obtained from static structure factor
                      measurements, our results of Monte Carlo simulations
                      representing seven experimental lysoyzme samples indicate
                      that they exist either in dispersed fluid or random
                      percolated states. The self-consistent Zerah-Hansen scheme
                      is used to describe the static structure factor, S(q), which
                      is the input to our calculation schemes for the short-time
                      hydrodynamic function, H(q), and the zero-frequency
                      viscosity η. The schemes account for hydrodynamic
                      interactions included on an approximate level. Theoretical
                      predictions for H(q) as a function of the wavenumber q
                      quantitatively agree with experimental results at small
                      protein concentrations obtained using neutron spin echo
                      measurements. At higher concentrations, qualitative
                      agreement is preserved although the calculated hydrodynamic
                      functions are overestimated. We attribute the differences
                      for higher concentrations and lower temperatures to
                      translational-rotational diffusion coupling induced by the
                      shape and interaction anisotropy of particles and clusters,
                      patchiness of the lysozyme particle surfaces, and the
                      intra-cluster dynamics, features not included in our simple
                      globular particle model. The theoretical results for the
                      solution viscosity, η, are in qualitative agreement with
                      our experimental data even at higher concentrations. We
                      demonstrate that semi-quantitative predictions of diffusion
                      properties and viscosity of solutions of globular proteins
                      are possible given only the equilibrium structure factor of
                      proteins. Furthermore, we explore the effects of changing
                      the attraction strength on H(q) and η},
      cin          = {ICS-3},
      ddc          = {530},
      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:29448794},
      UT           = {WOS:000425299800035},
      doi          = {10.1063/1.5016517},
      url          = {https://juser.fz-juelich.de/record/862616},
}