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@ARTICLE{Stadler:186273,
      author       = {Stadler, Andreas and Koza, Michael Marek and Fitter, Jörg},
      title        = {{D}etermination of {C}onformational {E}ntropy of {F}ully
                      and {P}artially {F}olded {C}onformations of {H}olo- and
                      {A}pomyoglobin},
      journal      = {The journal of physical chemistry / B},
      volume       = {119},
      number       = {1},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2015-00357},
      pages        = {72 - 82},
      year         = {2015},
      abstract     = {Holo- and apomyoglobin can be stabilized in native folded,
                      partially folded molten globules (MGs) and denatured states
                      depending on the solvent composition. Although the protein
                      has been studied as a model system in the field of protein
                      folding, little is known about the internal dynamics of the
                      different structural conformations on the picosecond time
                      scale. In a comparative experimental study we investigated
                      the correlation between protein folding and dynamics on the
                      picosecond time scale using incoherent quasielastic neutron
                      scattering (QENS). The measured mean square displacements
                      (MSDs) of conformational motions depend significantly on the
                      secondary structure content of the protein, whereas the
                      correlation times of the observed internal dynamics were
                      found to be similar irrespective of the degree of folding.
                      The conformational entropy difference ΔSconf between the
                      folded conformations and the acid denatured state could be
                      determined from the measured MSDs and was compared to the
                      entropy difference ΔS obtained from thermodynamic
                      parameters reported in the literature. The observed
                      difference between ΔS and ΔSconf was attributed to the
                      entropy difference ΔShydr of dynamically disordered water
                      molecules of the hydration shell. The entropy content of the
                      hydration water is significantly larger in the native folded
                      proteins than in the partially folded MGs. We demonstrate
                      the potential of incoherent neutron scattering for the
                      investigation of the role of conformational dynamics in
                      protein folding.},
      cin          = {ICS-5 / Neutronenstreuung ; JCNS-1 / ICS-1 / JCNS
                      (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-5-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)ICS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218},
      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)External-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000347753900009},
      doi          = {10.1021/jp509732q},
      url          = {https://juser.fz-juelich.de/record/186273},
}