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@ARTICLE{Hong:154750,
      author       = {Hong, Liang and Sharp, $Melissa\&nbsp$ and Poblete, Simón
                      and Biehl, Ralf and Zamponi, Michaela and Szekely, Noemi and
                      Appavou, Marie-Sousai and Winkler, Roland G. and Nauss,
                      Rachel E. and Johs, Alexander and Parks, $Jerry\&nbsp$ and
                      Yi, Zheng and Cheng, Xiaolin and Liang, Liyuan and Ohl,
                      Michael and Miller, $Susan\&nbsp$ and Richter, Dieter and
                      Gompper, Gerhard and Smith, $Jeremy\&nbsp$},
      title        = {{S}tructure and {D}ynamics of a {C}ompact {S}tate of a
                      {M}ultidomain {P}rotein, the {M}ercuric {I}on {R}eductase},
      journal      = {Biophysical journal},
      volume       = {107},
      number       = {2},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {FZJ-2014-04030},
      pages        = {393 - 400},
      year         = {2014},
      abstract     = {The functional efficacy of colocalized, linked protein
                      domains is dependent on linker flexibility and system
                      compaction. However, the detailed characterization of these
                      properties in aqueous solution presents an enduring
                      challenge. Here, we employ a novel, to our knowledge,
                      combination of complementary techniques, including
                      small-angle neutron scattering, neutron spin-echo
                      spectroscopy, and all-atom molecular dynamics and
                      coarse-grained simulation, to identify and characterize in
                      detail the structure and dynamics of a compact form of
                      mercuric ion reductase (MerA), an enzyme central to
                      bacterial mercury resistance. MerA possesses
                      metallochaperone-like N-terminal domains (NmerA) tethered to
                      its catalytic core domain by linkers. The NmerA domains are
                      found to interact principally through electrostatic
                      interactions with the core, leashed by the linkers so as to
                      subdiffuse on the surface over an area close to the core
                      C-terminal Hg(II)-binding cysteines. How this compact,
                      dynamical arrangement may facilitate delivery of Hg(II) from
                      NmerA to the core domain is discussed.},
      cin          = {ICS-1 / Neutronenstreuung ; JCNS-1 / JCNS (München) ;
                      Jülich Centre for Neutron Science JCNS (München) ;
                      JCNS-FRM-II / ICS-2 / IAS-2 / JCNS-SNS},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)ICS-2-20110106 / I:(DE-Juel1)IAS-2-20090406 /
                      I:(DE-Juel1)JCNS-SNS-20110128},
      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)J-NSE-20140101 / EXP:(DE-MLZ)KWS1-20140101 /
                      EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000339148500015},
      pubmed       = {pmid:25028881},
      doi          = {10.1016/j.bpj.2014.06.013},
      url          = {https://juser.fz-juelich.de/record/154750},
}