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@ARTICLE{Anghel:852482,
      author       = {Anghel, Lilia and Radulescu, Aurel and Erhan, Raul Victor},
      title        = {{S}tructural aspects of human lactoferrin in the
                      iron-binding process studied by molecular dynamics and
                      small-angle neutron scattering},
      journal      = {The European physical journal / E},
      volume       = {41},
      number       = {9},
      issn         = {1292-895X},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {FZJ-2018-05413},
      pages        = {109},
      year         = {2018},
      abstract     = {Lactoferrin is a non-heme protein known for its ability to
                      bind tightly Fe(III) ions in various physiological
                      environments. Due to this feature lactoferrin plays an
                      important role in the processes of iron regulation at the
                      cellular level preventing the body from damages produced by
                      high levels of free iron ions. The X-ray crystal structure
                      of human lactoferrin shows that the iron-binding process
                      leads to conformational changes within the protein
                      structure. The present study was addressed to conformation
                      stability of human lactoferrin in solution. Using molecular
                      dynamics simulations, it was shown that Arg121 is the key
                      amino acid in the stabilization of the Fe(III) ion in the
                      N-lobe of human lactoferrin. The small-angle neutron
                      scattering method allowed us to detect the structural
                      differences between the open and closed conformation of
                      human lactoferrin in solution. Our results indicate that the
                      radius of gyration of apolactoferrin appears to be smaller
                      than that of the hololactoferrin, Rg=24.16(±0.707) Å and
                      Rg=26.20(±1.191) Å, respectively. The low-resolution
                      three-dimensional models computed for both forms of human
                      lactoferrin in solution also show visible differences, both
                      having a more compact conformation compared to the
                      high-resolution structure.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {530},
      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)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30229350},
      UT           = {WOS:000444878400002},
      doi          = {10.1140/epje/i2018-11720-x},
      url          = {https://juser.fz-juelich.de/record/852482},
}