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@ARTICLE{Koutsioumpas:138629,
      author       = {Koutsioumpas, Alexandros and Berthaud, Alice and Mangenot,
                      Stephanie and Perez, Javier},
      title        = {{A}b {I}nitio and {A}ll-{A}tom {M}odeling of {D}etergent
                      {O}rganization around {A}quaporin-0 {B}ased on {SAXS}
                      {D}ata},
      journal      = {The journal of physical chemistry / B},
      volume       = {117},
      number       = {43},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2013-04727},
      pages        = {13588–13594},
      year         = {2013},
      abstract     = {A necessary initial step for the application of small angle
                      X-ray scattering (SAXS) as an analytical probe for
                      structural investigations of membrane proteins in solution
                      is the precise knowledge of the structure of spontaneously
                      formed detergent assemblies around the protein. Following
                      our recent article (Berthaud et al. J. Am. Chem. Soc. 2012,
                      134, 10080–10088) on the study of the n-dodecyl
                      β-d-maltopyranoside (dDM) corona surrounding Aquaporin-0
                      tetramers in solution, we aimed at the development of more
                      elaborate models, exploiting the information content of the
                      scattering data. Two additional approaches are developed
                      here for the fit of SAXS experimental data, one based on a
                      generalized ab initio algorithm for the construction of a
                      coarse-grained representation of the detergent assemblies,
                      and a second based on atomistic molecular dynamics.
                      Accordingly, we are able to fit the SAXS experimental data
                      and obtain a better insight concerning the structure of the
                      detergent corona around the hydrophobic part of the
                      Aquaporin-0 surface. The present analysis scheme represents
                      an additional step toward future conformational studies of
                      transmembrane proteins in solution.},
      cin          = {ICS-1 / Neutronenstreuung ; JCNS-1 / JCNS (München) ;
                      Jülich Centre for Neutron Science JCNS (München) ;
                      JCNS-FRM-II},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218},
      pnm          = {451 - Soft Matter Composites (POF2-451) / 54G - JCNS
                      (POF2-54G24)},
      pid          = {G:(DE-HGF)POF2-451 / G:(DE-HGF)POF2-54G24},
      experiment   = {EXP:(DE-MLZ)External-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000326608500022},
      pubmed       = {pmid:24144436},
      doi          = {10.1021/jp407688x},
      url          = {https://juser.fz-juelich.de/record/138629},
}