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@ARTICLE{Babcock:139042,
      author       = {Babcock, E. and Salhi, Z. and Appavou, M. -S. and
                      Feoktystov, A. and Pipich, V. and Radulescu, A. and Ossovyi,
                      V. and Staringer, S. and Ioffe, A.},
      title        = {{P}olarization {A}nalysis with 3{H}e {S}pin {F}ilters for
                      {S}eparating {C}oherent from {I}ncoherent {S}cattering in
                      {S}oft {M}atter {S}tudies},
      journal      = {Physics procedia},
      volume       = {42},
      issn         = {1875-3892},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2013-05063},
      pages        = {154 - 162},
      year         = {2013},
      abstract     = {In soft matter small angle neutron scattering (SANS)
                      studies at large Q values, incoherent scattering becomes the
                      dominant signal. In the Q-range of interest to this work,
                      from 0.2 Å−1 to about 1.0 Å−1, the coherent scattering
                      from the typical protein or polymer in a D2O buffer solution
                      inevitably drops one to two orders of magnitude or more
                      below the total scattering. Even after careful and accurate
                      subtraction of the measured D2O buffer scattering, the
                      remaining corrected, i.e. sample-only, signal will still be
                      dominated by diffuse incoherent scattering from hydrogen in
                      the sample itself. This is the exact region of interest when
                      one wishes to probe the structural changes in “living”
                      proteins caused by interactions and motions related to
                      function. To further complicate the problem, there is strong
                      motivation to measure this Q-regime at very low
                      concentrations because it has been shown with wide angle
                      X-ray scattering that proteins can undergo
                      concentration-dependent structural changes that rapidly
                      increase below concentrations of about $5\%$ [1] motivating
                      the study of protein solutions at ever lower concentrations.
                      In this case the signal from the protein will inevitably
                      become much less than the scattering of the D2O buffer
                      solution it is contained in. Polarization analysis offers
                      the opportunity to separate the weak coherent signal from
                      the larger incoherent signal and perhaps enable measurements
                      under the conditions described above. This paper will
                      address the issues associated with the correct separation of
                      coherent and incoherent scattering for soft matter samples.
                      We have performed tests measurements on KWS2 which show the
                      viability of the method on a protonated α-lactalbumin
                      solution at $2.5\%$ (1 mm thick) and $0.25\%$ (2 mm thick)
                      concentrations in a D2O buffer solution. Additionally
                      describe a the method of implementation using 3He spin
                      filters, some practical considerations, and future plans for
                      a dedicated device at the JCNS.},
      cin          = {PGI-4 / Neutronenstreuung ; JCNS-1 / JCNS-2 / JCNS
                      (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / JARA-FIT / ICS-1},
      ddc          = {530},
      cid          = {I:(DE-Juel1)PGI-4-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-2-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      $I:(DE-82)080009_20140620$ / I:(DE-Juel1)ICS-1-20110106},
      pnm          = {422 - Spin-based and quantum information (POF2-422) / 424 -
                      Exploratory materials and phenomena (POF2-424) / 542 -
                      Neutrons (POF2-542) / 544 - In-house Research with PNI
                      (POF2-544) / 54G - JCNS (POF2-54G24) / 451 - Soft Matter
                      Composites (POF2-451)},
      pid          = {G:(DE-HGF)POF2-422 / G:(DE-HGF)POF2-424 /
                      G:(DE-HGF)POF2-542 / G:(DE-HGF)POF2-544 /
                      G:(DE-HGF)POF2-54G24 / G:(DE-HGF)POF2-451},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000331183800024},
      doi          = {10.1016/j.phpro.2013.03.190},
      url          = {https://juser.fz-juelich.de/record/139042},
}