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@INPROCEEDINGS{Appavou:821022,
      author       = {Appavou, Marie-Sousai},
      title        = {{I}nfluence of pressure on proteins structure and dynamics
                      investigated by neutron scattering},
      reportid     = {FZJ-2016-06279},
      year         = {2016},
      abstract     = {Pressure is a physical parameter which influence is widely
                      spread in Earth. Indeed, micro-organisms like Bacillus
                      Licheniformis can live in Deep Ocean until 10 km and they
                      can sustain pressure of about 1000 bar [1]. Multimeric
                      protein subunits association-dissociation phenomena and
                      protein folding and unfolding is also more studied using
                      this unusual parameter. The interest of using high pressure
                      comes for its use in food industries for sterilization
                      process since this procedure has less influence on texture
                      and taste than thermal sterilization. In medicine, high
                      pressure is studied for bio-conservation of blood or other
                      oxygen transporter molecules for exampleSmall angle neutron
                      scattering is a suitable tool to investigate soft matter
                      material: for example, proteins from their native to their
                      fully unfolded state since the technique is not destructive
                      and model based on polymer theory studies can be adapted to
                      characterize the structures. The JCNS at MLZ has a 5000 bar
                      high pressure with sapphire windows especially dedicated for
                      structural investigation of soft matter, and particularly
                      biology, investigated by Small Angle Neutron Scattering. The
                      design is based on the high pressure set up described in
                      Kohlbrecher et al 2007 [2]. The cell will be described and a
                      typical example will be presented.Quasielastic neutron
                      scattering allows to explore at the atomic space scale
                      internal motions of proteins in the pico-second time scale
                      [3,4]. Few neutron scattering studies on biomolecules were
                      performed up to date. The first unfolding study using
                      inelastic neutron scattering was published by Doster et al
                      [5,6]. Other studies have been performed by Appavou et al
                      for BPTI [7] and by Di Bari for Trypsin [8]. We would like
                      to present a series of results as a function of pressure we
                      have obtained with the TOFTOF time of flight quasielastic
                      neutron scattering spectrometer (Garching, Germany).We have
                      built a high pressure cell which can sustain a pressure of
                      2000 bar. The high transmission, due to the aluminium alloy
                      of the cell, allows us to make a quite accurate observation
                      of the influence of pressure on the translational diffusion
                      and the internal dynamics of haemoglobin.References1. C.
                      Balny, Bull. Soc. Fr. Biophys. 140 10–13 (2003).2.
                      Kohlbrecher, J., et al., Rev. Sci. Instr. 78, 125101, doi:
                      10.1063/1.2817632 (2007)3. J.A. McCammon, S.C. Harvey,
                      Cambridge University Press, Cambridge, 29 (1988).4. M. Bée,
                      Adam Hilger, Bristol, (1988).5. W. Doster and W. Gebhardt,
                      Chem. Phys. 292, 383-389 (2003).6. W. Doster, R. Gebhardt
                      and A. Soper in: Advances in High Pressure Science and
                      Biotechnology II, Springer, Ed. R. Winter 29 (2003).7. M.-S.
                      Appavou, G. Gibrat, M.-C. Bellissent-Funel, Biochimica et
                      Biophysica Acta 1764 414–423 (2006).8. M. Di Bari, A.
                      Deriu, A. Filabozzi, C. Andreani, A. Di Venere, N. Rosato,
                      Physica B 276–278 510–511 (2000).},
      month         = {Sep},
      date          = {2016-09-20},
      organization  = {German Conference on Neutron
                       Scattering 2016, Kiel (Germany), 20 Sep
                       2016 - 22 Sep 2016},
      subtyp        = {Invited},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(DE-HGF)POF3-6G15 /
                      G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101 / EXP:(DE-MLZ)TOF-TOF-20140101},
      typ          = {PUB:(DE-HGF)6},
      url          = {https://juser.fz-juelich.de/record/821022},
}