% 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{Fitter:30449,
      author       = {Fitter, J.},
      title        = {{C}onformational dynamics of a protein in the folded and
                      unfolded state},
      journal      = {Chemical physics},
      volume       = {292},
      issn         = {0301-0104},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PreJuSER-30449},
      pages        = {405 - 411},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {In a quasielastic neutron scattering experiment, the
                      picosecond dynamics of alpha-amylase was investigated for
                      the folded and the unfolded state of the protein. In order
                      to ensure a reasonable interpretation of the internal
                      protein dynamics, the protein was measured in D2O-buffer
                      solution. The much higher structural flexibility of the pH
                      induced unfolded state as compared to the native folded
                      state was quantified using a simple analytical model,
                      describing a local diffusion inside a sphere. In terms of
                      this model the conformational volume, which is explored
                      mainly by confined protein side-chain movements, is
                      parameterized by the radius of a sphere (folded state, r =
                      1.2 Angstrom; unfolded state, 1.8 Angstrom). Differences in
                      conformational dynamics between the folded and the unfolded
                      state of a protein are of fundamental interest in the field
                      of protein science, because they are assumed to play an
                      important role for the thermodynamics of folding/unfolding
                      transition and for protein stability. (C) 2003 Elsevier
                      Science B.V. All rights reserved.},
      keywords     = {J (WoSType)},
      cin          = {IBI-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Chemistry, Physical / Physics, Atomic, Molecular $\&$
                      Chemical},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000184511200032},
      doi          = {10.1016/S0301-0104(03)00144-7},
      url          = {https://juser.fz-juelich.de/record/30449},
}