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@ARTICLE{Sarter:866680,
      author       = {Sarter, Mona and Niether, Doreen and König, Bernd and
                      Lohstroh, Wiebke and Zamponi, Michaela and Jalarvo, Niina H.
                      and Wiegand, Simone and Fitter, Jörg and Stadler, Andreas
                      M.},
      title        = {{S}trong {A}dverse {C}ontribution of {C}onformational
                      {D}ynamics to {S}treptavidin-{B}iotin {B}inding},
      journal      = {The journal of physical chemistry / B},
      volume       = {124},
      number       = {2},
      issn         = {1089-5647},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2019-05758},
      pages        = {324-335},
      year         = {2020},
      abstract     = {Molecular dynamics plays an important role for the
                      biological function of proteins. For protein ligand
                      interactions, changes of conformational entropy of protein
                      and hydration layer are relevant for the binding process.
                      Quasielastic neutron scattering (QENS) was used to
                      investigate differences in protein dynamics and
                      conformational entropy of ligand-bound and ligand-free
                      streptavidin. Protein dynamics were probed both on the fast
                      picosecond time scale using neutron time-of-flight
                      spectroscopy and on the slower nanosecond time scale using
                      high-resolution neutron backscattering spectroscopy. We
                      found the internal equilibrium motions of streptavidin and
                      the corresponding mean square displacements (MSDs) to be
                      greatly reduced upon biotin binding. On the basis of the
                      observed MSDs, we calculated the difference of
                      conformational entropy ΔSconf of the protein component
                      between ligand-bound and ligand-free streptavidin. The
                      rather large negative ΔSconf value (−2 kJ mol–1 K–1
                      on the nanosecond time scale) obtained for the streptavidin
                      tetramer seems to be counterintuitive, given the
                      exceptionally high affinity of streptavidin–biotin
                      binding. Literature data on the total entropy change ΔS
                      observed upon biotin binding to streptavidin, which includes
                      contributions from both the protein and the hydration water,
                      suggest partial compensation of the unfavorable ΔSconf by a
                      large positive entropy gain of the surrounding hydration
                      layer and water molecules that are displaced during ligand
                      binding.},
      cin          = {ICS-5 / ICS-3 / ICS-6 / JCNS-1 / JCNS-SNS / ICS-1 /
                      JCNS-FRM-II},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-5-20110106 / I:(DE-Juel1)ICS-3-20110106 /
                      I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-SNS-20110128 / I:(DE-Juel1)ICS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      experiment   = {EXP:(DE-MLZ)SPHERES-20140101 /
                      EXP:(DE-MLZ)TOF-TOF-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31710813},
      UT           = {WOS:000508468600003},
      doi          = {10.1021/acs.jpcb.9b08467},
      url          = {https://juser.fz-juelich.de/record/866680},
}