% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Mueller:255496,
      author       = {Mueller, Thomas and Groot, Joost de and Strempfer, Jörg
                      and Angst, Manuel},
      title        = {{S}toichiometric {YF}e2{O}4−δ single crystals grown by
                      the optical floating zone method},
      journal      = {Journal of crystal growth},
      volume       = {428},
      issn         = {0022-0248},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2015-05658},
      pages        = {40 - 45},
      year         = {2015},
      abstract     = {Large-scale domain motions in alcohol dehydrogenase (ADH)
                      have been observed previously by neutron spin-echo
                      spectroscopy (NSE). We have extended the investigation on
                      the dynamics of ADH in solution by using high-resolution
                      neutron time-of-flight (TOF) and neutron backscattering (BS)
                      spectroscopy in the incoherent scattering range. The
                      observed hydrogen dynamics were interpreted in terms of
                      three mobility classes, which allowed a simultaneous
                      description of the measured TOF and BS spectra. In addition
                      to the slow global protein diffusion and domain motions
                      observed by NSE, a fast internal process could be
                      identified. Around one third of the protons in ADH
                      participate in the fast localized diffusive motion. The
                      diffusion coefficient of the fast internal motions is around
                      two third of the value of the surrounding D2O solvent. It is
                      tempting to associate the fast internal process with solvent
                      exposed amino acid residues with dangling side chains.},
      cin          = {JCNS-2 / PGI-4 / JARA-FIT},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-2-20110106 / I:(DE-Juel1)PGI-4-20110106 /
                      $I:(DE-82)080009_20140620$},
      pnm          = {144 - Controlling Collective States (POF3-144) / 524 -
                      Controlling Collective States (POF3-524) / 6212 - Quantum
                      Condensed Matter: Magnetism, Superconductivity (POF3-621) /
                      6213 - Materials and Processes for Energy and Transport
                      Technologies (POF3-621) / 6G4 - Jülich Centre for Neutron
                      Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-144 / G:(DE-HGF)POF3-524 /
                      G:(DE-HGF)POF3-6212 / G:(DE-HGF)POF3-6213 /
                      G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-H253)P-P09-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000360501200007},
      doi          = {10.1016/j.jcrysgro.2015.07.015},
      url          = {https://juser.fz-juelich.de/record/255496},
}