% 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{Stadler:4704,
      author       = {Stadler, A.M. and Digel, I. and Embs, J.P. and Unruh, T.
                      and Zaccai, G. and Büldt, G. and Artmann, G.},
      title        = {{F}rom {P}owder to {S}olution: {H}emoglobin {D}ynamics
                      {C}orrelated to {B}ody {T}emperature},
      journal      = {Biophysical journal},
      volume       = {96},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-4704},
      pages        = {5073 - 5081},
      year         = {2009},
      note         = {This work was supported by the European Commission under
                      the 6th Framework Programme through the Key Action:
                      Strengthening the European Research Area, Research
                      Infrastructures (RII3-CT-2003-505925), the Institut
                      Laue-Langevin (M.T.), and the AINSE (M.T.).},
      abstract     = {A transition in hemoglobin (Hb), involving partial
                      unfolding and aggregation, has been shown previously by
                      various biophysical methods. The correlation between the
                      transition temperature and body temperature for Hb from
                      different species, suggested that it might be significant
                      for biological function. To focus on such biologically
                      relevant human Hb dynamics, we studied the protein internal
                      picosecond motions as a response to hydration, by elastic
                      and quasielastic neutron scattering. Rates of fast diffusive
                      motions were found to be significantly enhanced with
                      increasing hydration from fully hydrated powder to
                      concentrated Hb solution. In concentrated protein solution,
                      the data showed that amino acid side chains can explore
                      larger volumes above body temperature than expected from
                      normal temperature dependence. The body temperature
                      transition in protein dynamics was absent in fully hydrated
                      powder, indicating that picosecond protein dynamics
                      responsible for the transition is activated only at a
                      sufficient level of hydration. A collateral result from the
                      study is that fully hydrated protein powder samples do not
                      accurately describe all aspects of protein picosecond
                      dynamics that might be necessary for biological function.},
      keywords     = {Body Temperature / Elasticity / Hemoglobins: chemistry /
                      Humans / Neutrons / Powders / Solutions / Water: chemistry /
                      Hemoglobins (NLM Chemicals) / Powders (NLM Chemicals) /
                      Solutions (NLM Chemicals) / Water (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ISB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {Programm Biosoft},
      pid          = {G:(DE-Juel1)FUEK443},
      experiment   = {EXP:(DE-MLZ)TOF-TOF-20140101},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19527667},
      pmc          = {pmc:PMC2712052},
      UT           = {WOS:000267194600032},
      doi          = {10.1016/j.bpj.2009.03.043},
      url          = {https://juser.fz-juelich.de/record/4704},
}