% 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:155323,
      author       = {Stadler, Andreas and Garvey, Christopher J. and Embs, Jan
                      Peter and Koza, Michael Marek and Unruh, Tobias and Artmann,
                      Gerhard and Zaccai, Giuseppe},
      title        = {{P}icosecond dynamics in haemoglobin from different
                      species: {A} quasielastic neutron scattering study},
      journal      = {Biochimica et biophysica acta / General subjects},
      volume       = {1840},
      number       = {10},
      issn         = {0304-4165},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2014-04496},
      pages        = {2989 - 2999},
      year         = {2014},
      abstract     = {BackgroundDynamics in haemoglobin from platypus
                      (Ornithorhynchus anatinus), chicken (Gallus gallus
                      domesticus) and saltwater crocodile (Crocodylus porosus)
                      were measured to investigate response of conformational
                      motions on the picosecond time scale to naturally occurring
                      variations in the amino acid sequence of structurally
                      identical proteins.MethodsProtein dynamics was measured
                      using incoherent quasielastic neutron scattering. The
                      quasielastic broadening was interpreted first with a simple
                      single Lorentzian approach and then by using the
                      Kneller–Volino Brownian dynamics model.ResultsMean square
                      displacements of conformational motions, diffusion
                      coefficients of internal dynamics and residence times for
                      jump-diffusion between sites and corresponding effective
                      force constants (resilience) and activation energies were
                      determined from the data.ConclusionsModifications of the
                      physicochemical properties caused by mutations of the amino
                      acids were found to have a significant impact on protein
                      dynamics. Activation energies of local side chain dynamics
                      were found to be similar between the different proteins
                      being close to the energy, which is required for the rupture
                      of single hydrogen bond in a protein.General significanceThe
                      measured dynamic quantities showed significant and
                      systematic variations between the investigated species,
                      suggesting that they are the signature of an evolutionary
                      adaptation process stimulated by the different physiological
                      environments of the respective protein.},
      cin          = {ICS-1 / Neutronenstreuung ; JCNS-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {451 - Soft Matter Composites (POF2-451) / 54G - JCNS
                      (POF2-54G24)},
      pid          = {G:(DE-HGF)POF2-451 / G:(DE-HGF)POF2-54G24},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000341675900001},
      doi          = {10.1016/j.bbagen.2014.06.007},
      url          = {https://juser.fz-juelich.de/record/155323},
}