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@ARTICLE{DosSantosMorais:838848,
      author       = {Dos Santos Morais, Raphael and Delalande, Olivier and
                      Pérez, Javier and Mouret, Liza and Bondon, Arnaud and
                      Martel, Anne and Appavou, Marie-Sousai and Le Rumeur,
                      Elisabeth and Hubert, Jean-François and Combet, Sophie},
      title        = {{C}ontrast-{M}atched {I}sotropic {B}icelles: {A}
                      {V}ersatile {T}ool to {S}pecifically {P}robe the {S}olution
                      {S}tructure of {P}eripheral {M}embrane {P}roteins {U}sing
                      {SANS}},
      journal      = {Langmuir},
      volume       = {33},
      number       = {26},
      issn         = {1520-5827},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2017-07358},
      pages        = {6572 - 6580},
      year         = {2017},
      abstract     = {Obtaining structural information on integral or peripheral
                      membrane proteins is currently arduous due to the difficulty
                      of their solubilization, purification, and crystallization
                      (for X-ray crystallography (XRC) application). To overcome
                      this challenge, bicelles are known to be a versatile tool
                      for high-resolution structure determination, especially when
                      using solution and/or solid state nuclear magnetic resonance
                      (NMR) and, to a lesser extent, XRC. For proteins not
                      compatible with these high-resolution methods, small-angle
                      X-ray and neutron scattering (SAXS and SANS, respectively)
                      are powerful alternatives to obtain structural information
                      directly in solution. In particular, the SANS-based approach
                      is a unique technique to obtain low-resolution structures of
                      proteins in interactions with partners by contrast-matching
                      the signal coming from the latter. In the present study,
                      isotropic bicelles are used as a membrane mimic model for
                      SANS-based structural studies of bound peripheral membrane
                      proteins. We emphasize that the SANS signal coming from the
                      deuterated isotropic bicelles can be contrast-matched in
                      $100\%$ D2O-based buffer, allowing us to separately and
                      specifically focus on the signal coming from the protein in
                      interaction with membrane lipids. We applied this method to
                      the DYS-R11–15 protein, a fragment of the central domain
                      of human dystrophin known to interact with lipids, and we
                      were able to recover the signal from the protein alone. This
                      approach gives rise to new perspectives to determine the
                      solution structure of peripheral membrane proteins
                      interacting with lipid membranes and might be extended to
                      integral membrane proteins.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {670},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      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)KWS1-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28581294},
      UT           = {WOS:000405057100014},
      doi          = {10.1021/acs.langmuir.7b01369},
      url          = {https://juser.fz-juelich.de/record/838848},
}