% 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{Fabiani:4699,
      author       = {Fabiani, E. and Stadler, A.M. and Madern, D. and Hirai, M.
                      and Zaccai, G.},
      title        = {{D}ynamics of apo-myoglobin in the alpha-to-beta transition
                      and of partially unfolded aggregated protein},
      journal      = {European biophysics journal},
      volume       = {38},
      issn         = {0175-7571},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {PreJuSER-4699},
      pages        = {237 - 244},
      year         = {2009},
      note         = {The authors acknowledge the IN13 and IRIS staffs for their
                      support during the experiment at ILL and ISIS facilities.
                      Thanks are due to Dr. Felix Fernandez-Alonso and Dr. Franz
                      Demmel for helpful discussions. Technical and financial
                      support from the ILL and ISIS facilities is gratefully
                      acknowledged. The WAXS measurement was done under the
                      approval of the JASRI Program Advisory Committee ( Proposal
                      #2006A1339). M. Tehei acknowledges the ILL, the AINSE, the
                      CNRS and the Institut de Biologie Structurale (UMR 5075) for
                      financial support of this work.},
      abstract     = {Changes of molecular dynamics in the alpha-to-beta
                      transition associated with amyloid fibril formation were
                      explored on apomyoglobin (ApoMb) as a model system. Circular
                      dichroism, neutron and X-ray scattering experiments were
                      performed as a function of temperature on the protein, at
                      different solvent conditions. A significant change in
                      molecular dynamics was observed at the alpha-to-beta
                      transition at about 55 degrees C, indicating a more
                      resilient high temperature beta structure phase. A similar
                      effect at approximately the same temperature was observed in
                      holo-myoglobin, associated with partial unfolding and
                      protein aggregation. A study in a wide temperature range
                      between 20 and 360 K revealed that a dynamical transition at
                      about 200 K for motions in the 50 ps time scale exists also
                      for a hydrated powder of heat-denatured aggregated ApoMb.},
      keywords     = {Amyloidosis: physiopathology / Apoproteins: chemistry /
                      Circular Dichroism / Crystallography, X-Ray / Models,
                      Molecular / Myoglobin: chemistry / Neutron Diffraction /
                      Pharmaceutical Solutions / Protein Folding / Protein
                      Multimerization / Protein Structure, Tertiary / Temperature
                      / Thermodynamics / Apoproteins (NLM Chemicals) / Myoglobin
                      (NLM Chemicals) / Pharmaceutical Solutions (NLM Chemicals) /
                      apomyoglobin (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {Programm Biosoft},
      pid          = {G:(DE-Juel1)FUEK443},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18853152},
      UT           = {WOS:000262671600010},
      doi          = {10.1007/s00249-008-0375-z},
      url          = {https://juser.fz-juelich.de/record/4699},
}