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@ARTICLE{Ameseder:864773,
      author       = {Ameseder, Felix and Biehl, Ralf and Holderer, Olaf and
                      Richter, Dieter and Stadler, Andreas M.},
      title        = {{L}ocalised contacts lead to nanosecond hinge motions in
                      dimeric bovine serum albumin},
      journal      = {Physical chemistry, chemical physics},
      volume       = {21},
      number       = {34},
      issn         = {1463-9084},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {FZJ-2019-04440},
      pages        = {18477 - 18485},
      year         = {2019},
      abstract     = {Domain motions in proteins are crucial for biological
                      function. In the present manuscript, we present a neutron
                      spin-echo spectroscopy (NSE) study of native bovine serum
                      albumin (BSA) in solution. NSE allows to probe both global
                      and internal dynamics of the BSA monomer and dimer
                      equilibrium that is formed in solution. Using a model
                      independent approach, we were able to identify an internal
                      dynamic process in BSA that is visible in addition to global
                      rigid-body diffusion of the BSA monomer and dimer mixture.
                      The observed internal protein motion is characterised by a
                      relaxation time of 43 ns. The overdamped Brownian oscillator
                      was considered as an alternative analytical theory that was
                      able to describe the internal process as first-order
                      approximation. More detailed information on the physical
                      nature of the internal protein motion was extracted from the
                      q-dependent internal diffusion coefficients ΔDeff(q) that
                      were detected by NSE in addition to global rigid-body
                      translational and rotational diffusion. The ΔDeff(q) were
                      interpreted using normal mode analysis based on the
                      available crystal structures of the BSA monomer and dimer as
                      structural test models. Normal mode analysis demonstrates
                      that the observed internal dynamic process can be attributed
                      to bending motion of the BSA dimer. The native BSA monomer
                      does not show any internal dynamics on the time- and
                      length-scales probed by NSE. An intermolecular disulphide
                      bridge or a direct structural contact between the BSA
                      monomers forms a localised link acting as a molecular hinge
                      in the BSA dimer. The effect of that hinge on the observed
                      motion of BSA in the used dimeric structural model is
                      discussed in terms of normal modes in a molecular picture.},
      cin          = {JCNS-1 / ICS-1 / JCNS-FRM-II / MLZ},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)ICS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)J-NSE-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31210243},
      UT           = {WOS:000483701200034},
      doi          = {10.1039/C9CP01847F},
      url          = {https://juser.fz-juelich.de/record/864773},
}