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@ARTICLE{Sill:820572,
      author       = {Sill, Clemens and Biehl, Ralf and Hoffmann, Bernd and
                      Radulescu, Aurel and Appavou, Marie-Sousai and Farago, Bela
                      and Merkel, Rudolf and Richter, Dieter},
      title        = {{S}tructure and domain dynamics of human lactoferrin in
                      solution and the influence of {F}e({III})-ion ligand
                      binding},
      journal      = {BMC Biophysics},
      volume       = {9},
      number       = {1},
      issn         = {2046-1682},
      address      = {London},
      publisher    = {BioMed Central},
      reportid     = {FZJ-2016-05846},
      pages        = {7},
      year         = {2016},
      abstract     = {BackgroundHuman lactoferrin is an iron-binding protein of
                      the innate immune system consisting of two connected lobes,
                      each with a binding site located in a cleft. The clefts in
                      each lobe undergo a hinge movement from open to close when
                      Fe3+ is present in the solution and can be bound. The
                      binding mechanism was assumed to relate on thermal domain
                      fluctuations of the cleft domains prior to binding. We used
                      Small Angle Neutron Scattering and Neutron Spin Echo
                      Spectroscopy to determine the lactoferrin structure and
                      domain dynamics in solution.ResultsWhen Fe3+ is present in
                      solution interparticle interactions change from repulsive to
                      attractive in conjunction with emerging metas aggregates,
                      which are not observed without Fe3+. The protein form factor
                      shows the expected change due to lobe closing if Fe3+ is
                      present. The dominating motions of internal domain dynamics
                      with relaxation times in the 30–50 ns range show strong
                      bending and stretching modes with a steric suppressed
                      torsion, but are almost independent of the cleft
                      conformation. Thermally driven cleft closing motions of
                      relevant amplitude are not observed if the cleft is
                      open.ConclusionThe Fe3+ binding mechanism is not related to
                      thermal equilibrium fluctuations closing the cleft. A likely
                      explanation may be that upon entering the cleft the iron ion
                      first binds weakly which destabilizes and softens the hinge
                      region and enables large fluctuations that then close the
                      cleft resulting in the final formation of the stable iron
                      binding site and, at the same time, stable closed
                      conformation.},
      cin          = {ICS-7 / JCNS-2 / JCNS (München) ; Jülich Centre for
                      Neutron Science JCNS (München) ; JCNS-FRM-II},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-7-20110106 / I:(DE-Juel1)JCNS-2-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101 / EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000388036600001},
      doi          = {10.1186/s13628-016-0032-3},
      url          = {https://juser.fz-juelich.de/record/820572},
}