% 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{Calligari:205012,
      author       = {Calligari, Paolo A. and Calandrini, Vania and Ollivier,
                      Jacques and Artero, Jean-Baptiste and Härtlein, Michael and
                      Johnson, Mark and Kneller, Gerald R.},
      title        = {{A}daptation of {E}xtremophilic {P}roteins with
                      {T}emperature and {P}ressure: {E}vidence from {I}nitiation
                      {F}actor 6},
      journal      = {The journal of physical chemistry / B},
      volume       = {119},
      number       = {25},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2015-05517},
      pages        = {7860 - 7873},
      year         = {2015},
      abstract     = {In this work, we study dynamical properties of an
                      extremophilic protein, Initiation Factor 6 (IF6), produced
                      by the archeabacterium Methanocaldococcus jannascii, which
                      thrives close to deep-sea hydrothermal vents where
                      temperatures reach 80 °C and the pressure is up to 750 bar.
                      Molecular dynamics simulations (MD) and quasi-elastic
                      neutron scattering (QENS) measurements give new insights
                      into the dynamical properties of this protein with respect
                      to its eukaryotic and mesophilic homologue. Results obtained
                      by MD are supported by QENS data and are interpreted within
                      the framework of a fractional Brownian dynamics model for
                      the characterization of protein relaxation dynamics. IF6
                      from M. jannaschii at high temperature and pressure shares
                      similar flexibility with its eukaryotic homologue from S.
                      cerevisieae under ambient conditions. This work shows for
                      the first time, to our knowledge, that the very common
                      pattern of corresponding states for thermophilic protein
                      adaptation can be extended to thermo-barophilic proteins. A
                      detailed analysis of dynamic properties and of local
                      structural fluctuations reveals a complex pattern for
                      “corresponding” structural flexibilities. In particular,
                      in the case of IF6, the latter seems to be strongly related
                      to the entropic contribution given by an additional,
                      C-terminal, 20 amino-acid tail which is evolutionary
                      conserved in all mesophilic IF6s.},
      cin          = {GRS / IAS-5},
      ddc          = {530},
      cid          = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000357139800009},
      pubmed       = {pmid:25996652},
      doi          = {10.1021/acs.jpcb.5b02034},
      url          = {https://juser.fz-juelich.de/record/205012},
}