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@ARTICLE{Stadler:820002,
      author       = {Stadler, Andreas and Demmel, Franz and Ollivier, Jacques
                      and Seydel, Tilo},
      title        = {{P}icosecond to nanosecond dynamics provide a source of
                      conformational entropy for protein folding},
      journal      = {Physical chemistry, chemical physics},
      volume       = {18},
      number       = {31},
      issn         = {1463-9084},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {FZJ-2016-05569},
      pages        = {21527 - 21538},
      year         = {2016},
      abstract     = {Myoglobin can be trapped in fully folded structures,
                      partially folded molten globules, and unfolded states under
                      stable equilibrium conditions. Here, we report an
                      experimental study on the conformational dynamics of
                      different folded conformational states of apo- and
                      holomyoglobin in solution. Global protein diffusion and
                      internal molecular motions were probed by neutron
                      time-of-flight and neutron backscattering spectroscopy on
                      the picosecond and nanosecond time scales. Global protein
                      diffusion was found to depend on the α-helical content of
                      the protein suggesting that charges on the macromolecule
                      increase the short-time diffusion of protein. With regard to
                      the molten globules, a gel-like phase due to protein
                      entanglement and interactions with neighbouring
                      macromolecules was visible due to a reduction of the global
                      diffusion coefficients on the nanosecond time scale.
                      Diffusion coefficients, residence and relaxation times of
                      internal protein dynamics and root mean square displacements
                      of localised internal motions were determined for the
                      investigated structural states. The difference in
                      conformational entropy ΔSconf of the protein between the
                      unfolded and the partially or fully folded conformations was
                      extracted from the measured root mean square displacements.
                      Using thermodynamic parameters from the literature and the
                      experimentally determined ΔSconf values we could identify
                      the entropic contribution of the hydration shell ΔShydr of
                      the different folded states. Our results point out the
                      relevance of conformational entropy of the protein and the
                      hydration shell for stability and folding of myoglobin.},
      cin          = {ICS-1 / Neutronenstreuung ; JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106},
      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},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000381418000062},
      doi          = {10.1039/C6CP04146A},
      url          = {https://juser.fz-juelich.de/record/820002},
}