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@ARTICLE{Sonntag:838851,
      author       = {Sonntag, Miriam and Jagtap, Pravin Kumar Ankush and Simon,
                      Bernd and Appavou, Marie-Sousai and Geerlof, Arie and
                      Stehle, Ralf and Gabel, Frank and Hennig, Janosch and
                      Sattler, Michael},
      title        = {{S}egmental, {D}omain-{S}elective {P}erdeuteration and
                      {S}mall-{A}ngle {N}eutron {S}cattering for {S}tructural
                      {A}nalysis of {M}ulti-{D}omain {P}roteins},
      journal      = {Angewandte Chemie / International edition},
      volume       = {56},
      number       = {32},
      issn         = {1433-7851},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2017-07361},
      pages        = {9322 - 9325},
      year         = {2017},
      abstract     = {Multi-domain proteins play critical roles in fine-tuning
                      essential processes in cellular signaling and gene
                      regulation. Typically, multiple globular domains that are
                      connected by flexible linkers undergo dynamic rearrangements
                      upon binding to protein, DNA or RNA ligands. RNA binding
                      proteins (RBPs) represent an important class of multi-domain
                      proteins, which regulate gene expression by recognizing
                      linear or structured RNA sequence motifs. Here, we employ
                      segmental perdeuteration of the three RNA recognition motif
                      (RRM) domains in the RBP TIA-1 using Sortase A mediated
                      protein ligation. We show that domain-selective
                      perdeuteration combined with contrast-matched small-angle
                      neutron scattering (SANS), SAXS and computational modeling
                      provides valuable information to precisely define relative
                      domain arrangements. The approach is generally applicable to
                      study conformational arrangements of individual domains in
                      multi-domain proteins and changes induced by ligand
                      binding.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {540},
      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 / EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28636238},
      UT           = {WOS:000406385200010},
      doi          = {10.1002/anie.201702904},
      url          = {https://juser.fz-juelich.de/record/838851},
}