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@ARTICLE{Stadler:23114,
      author       = {Stadler, A.M. and Garvey, C.J. and Bocahut, A. and
                      Sacquin-Mora, S. and Digel, I. and Schneider, G.J. and
                      Natali, F. and Artmann, G.M. and Zaccai, G.},
      title        = {{T}hermal fluctuations of haemoglobin from different
                      species: adaptation to temperature via conformational
                      dynamics},
      journal      = {Interface},
      volume       = {9},
      issn         = {1742-5689},
      address      = {London},
      publisher    = {The Royal Society},
      reportid     = {PreJuSER-23114},
      pages        = {2845 - 2855},
      year         = {2012},
      note         = {Platypus RBC was provided by Nick Gust (Department of
                      Primary Industries Tasmania, Australia) and Dominic Geraghty
                      (University of Tasmania, Australia). Crocodile blood was
                      provided by Crocodylus Park (Darwin, Australia). We thank
                      Prof. Philip Kuchel (University of Sydney, Australia) for
                      the use of his laboratory to purify crocodile and platypus
                      Hb. Chicken blood was provided by Mario Suarez Avello and
                      Josefa Garcia Alvarez. I. D. was sponsored by the BMBF
                      Programme 'FHProfUnd' grant no. 1736X08. We also thank the
                      Ministry of Innovation Science and Research of the federal
                      state North Rhine-Westphalia for supporting Prof. Aysegul
                      (Temiz) Artmann's project Dynamischer Strukturubergang bei
                      Korpertemperaturen (FKZ: 800 009 04). A. M. S. thanks Prof.
                      Georg Buldt and Prof. Dieter Richter for continuous support.
                      This work is based on experiments performed at the Institute
                      Laue-Langevin (ILL), Grenoble, France, and at the
                      Forschungs-Neutronenquelle Heinz Maier-Leibnitz (FRM II),
                      Garching, Germany.},
      abstract     = {Thermodynamic stability, configurational motions and
                      internal forces of haemoglobin (Hb) of three endotherms
                      (platypus, Ornithorhynchus anatinus; domestic chicken,
                      Gallus gallus domesticus and human, Homo sapiens) and an
                      ectotherm (salt water crocodile, Crocodylus porosus) were
                      investigated using circular dichroism, incoherent elastic
                      neutron scattering and coarse-grained Brownian dynamics
                      simulations. The experimental results from Hb solutions
                      revealed a direct correlation between protein resilience,
                      melting temperature and average body temperature of the
                      different species on the 0.1 ns time scale. Molecular forces
                      appeared to be adapted to permit conformational fluctuations
                      with a root mean square displacement close to 1.2 Å at the
                      corresponding average body temperature of the endotherms.
                      Strong forces within crocodile Hb maintain the amplitudes of
                      motion within a narrow limit over the entire temperature
                      range in which the animal lives. In fully hydrated powder
                      samples of human and chicken, Hb mean square displacements
                      and effective force constants on the 1 ns time scale showed
                      no differences over the whole temperature range from 10 to
                      300 K, in contrast to the solution case. A complementary
                      result of the study, therefore, is that one hydration layer
                      is not sufficient to activate all conformational
                      fluctuations of Hb in the pico- to nanosecond time scale
                      which might be relevant for biological function.
                      Coarse-grained Brownian dynamics simulations permitted to
                      explore residue-specific effects. They indicated that
                      temperature sensing of human and chicken Hb occurs mainly at
                      residues lining internal cavities in the β-subunits.},
      keywords     = {J (WoSType)},
      cin          = {ICS-1 / JCNS-1 / JCNS (München) ; Jülich Centre for
                      Neutron Science JCNS (München) ; JCNS-FRM-II},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung / 544 - In-house Research with PNI
                      (POF2-544)},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-HGF)POF2-544},
      experiment   = {EXP:(DE-MLZ)SPHERES-20140101},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22696485},
      pmc          = {pmc:PMC3479923},
      UT           = {WOS:000309269100010},
      doi          = {10.1098/rsif.2012.0364},
      url          = {https://juser.fz-juelich.de/record/23114},
}