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@ARTICLE{Zhang:19773,
      author       = {Zhang, F. and Roosen-Runge, F. and Skoda, M.W.A. and
                      Jacobs, R.M.J. and Wolf, M. and Callow, P. and Frielinghaus,
                      H. and Pipich, V. and Prévost, S. and Schreiber, F.},
      title        = {{H}ydration and interactions in protein solutions
                      containing concentrated electrolytes studied by small-angle
                      scattering},
      journal      = {Physical Chemistry Chemical Physics},
      volume       = {14},
      issn         = {1463-9076},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {PreJuSER-19773},
      pages        = {2483 - 2493},
      year         = {2012},
      note         = {We gratefully acknowledge financial support from Deutsche
                      Forschungsgemeinschaft (DFG) and the beam time allocation
                      from ESRF, ILL, JCNS and Helmholtz-Center Berlin (BENSC).
                      The beam time on V4 at the Helmholtz Zentrum Berlin has been
                      supported by the European Commission under the 6th Framework
                      Program through the Key Action: Strengthening the European
                      Research Area, Research Infrastructures. Contract No.
                      RII3-CT-2003-505925 (NMI3).},
      abstract     = {During protein crystallization and purification, proteins
                      are commonly found in concentrated salt solutions. The exact
                      interplay of the hydration shell, the salt ions, and
                      protein-protein interactions under these conditions is far
                      from being understood on a fundamental level, despite the
                      obvious practical relevance. We have studied a model
                      globular protein (bovine serum albumin, BSA) in concentrated
                      salt solutions by small-angle neutron scattering (SANS). The
                      data are also compared to previous studies using SAXS. The
                      SANS results for dilute protein solutions give an averaged
                      volume of BSA of 91,700 Å(3), which is about $37\%$
                      smaller than that determined by SAXS. The difference in
                      volume corresponds to the contribution of a hydration shell
                      with a hydration level of 0.30 g g(-1) protein. The forward
                      intensity I(0) determined from Guinier analysis is used to
                      determine the second virial coefficient, A(2), which
                      describes the overall protein interactions in solution. It
                      is found that A(2) follows the reverse order of the
                      Hofmeister series, i.e. (NH(4))(2)SO(4) < Na(2)SO(4) < NaOAc
                      < NaCl < NaNO(3) < NaSCN. The dimensionless second virial
                      coefficient B(2), corrected for the particle volume and
                      molecular weight, has been calculated using different
                      approaches, and shows that B(2) with corrections for
                      hydration and the non-spherical shape of the protein
                      describes the interactions better than those determined from
                      the bare protein. SANS data are further analyzed in the full
                      q-range using liquid theoretical approaches, which gives
                      results consistent with the A(2) analysis and the
                      experimental structure factor.},
      keywords     = {Animals / Cattle / Electrolytes: chemistry / Neutron
                      Diffraction / Osmolar Concentration / Protein Interaction
                      Mapping / Salts: chemistry / Scattering, Small Angle / Serum
                      Albumin, Bovine: chemistry / X-Ray Diffraction /
                      Electrolytes (NLM Chemicals) / Salts (NLM Chemicals) / Serum
                      Albumin, Bovine (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-1 / JCNS (München) ; Jülich Centre for Neutron
                      Science JCNS (München) ; JCNS-FRM-II / JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung / Großgeräte für die Forschung
                      mit Photonen, Neutronen und Ionen (PNI)},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-Juel1)FUEK415},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101},
      shelfmark    = {Chemistry, Physical / Physics, Atomic, Molecular $\&$
                      Chemical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22249363},
      UT           = {WOS:000299505400046},
      doi          = {10.1039/c2cp23460b},
      url          = {https://juser.fz-juelich.de/record/19773},
}