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@ARTICLE{Stadler:763,
      author       = {Stadler, A.M. and Digel, I. and Artmann, G.M. and Embs,
                      J.P. and Zaccai, G. and Büldt, G.},
      title        = {{H}emoglobin {D}ynamics in {R}ed {B}lood {C}ells:
                      {C}orrelation to {B}ody {T}emperature},
      journal      = {Biophysical journal},
      volume       = {95},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-763},
      pages        = {5449 - 5461},
      year         = {2008},
      note         = {This research project was supported by the European
                      Commission under the 6th Framework Programme through Key
                      Action: Strengthening the European Research Area, Research
                      Infrastructures, contract No. RII3-CT-2003505925.},
      abstract     = {A transition in hemoglobin behavior at close to body
                      temperature has been discovered recently by micropipette
                      aspiration experiments on single red blood cells (RBCs) and
                      circular dichroism spectroscopy on hemoglobin solutions. The
                      transition temperature was directly correlated to the body
                      temperatures of a variety of species. In an exploration of
                      the molecular basis for the transition, we present neutron
                      scattering measurements of the temperature dependence of
                      hemoglobin dynamics in whole human RBCs in vivo. The data
                      reveal a change in the geometry of internal protein motions
                      at 36.9 degrees C, at human body temperature. Above that
                      temperature, amino acid side-chain motions occupy larger
                      volumes than expected from normal temperature dependence,
                      indicating partial unfolding of the protein. Global protein
                      diffusion in RBCs was also measured and the findings
                      compared favorably with theoretical predictions for
                      short-time self-diffusion of noncharged hard-sphere
                      colloids. The results demonstrated that changes in molecular
                      dynamics in the picosecond time range and angstrom length
                      scale might well be connected to a macroscopic effect on
                      whole RBCs that occurs at body temperature.},
      keywords     = {Body Temperature / Diffusion / Elasticity / Erythrocytes:
                      metabolism / Hemoglobins: metabolism / Humans / Neutron
                      Diffraction / Protein Denaturation / Hemoglobins (NLM
                      Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18708462},
      pmc          = {pmc:PMC2586580},
      UT           = {WOS:000260999500043},
      doi          = {10.1529/biophysj.108.138040},
      url          = {https://juser.fz-juelich.de/record/763},
}