% 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{Biehl:187631,
      author       = {Biehl, R. and Richter, D.},
      title        = {{S}low internal protein dynamics in solution},
      journal      = {Journal of physics / Condensed matter},
      volume       = {26},
      number       = {50},
      issn         = {1361-648X},
      address      = {Bristol},
      publisher    = {IOP Publ.},
      reportid     = {FZJ-2015-01257},
      pages        = {503103},
      year         = {2014},
      abstract     = {Large-scale domain dynamics in proteins are found when
                      flexible linkers or hinges connect domains. The related
                      conformational changes are often related to the function of
                      the protein, for example by arranging the active center
                      after substrate binding or allowing transport and release of
                      products. The adaptation of a specific active structure is
                      referred to as 'induced fit' and is challenged by models
                      such as 'conformational sampling'. Newer models about
                      protein function include some flexibility within the protein
                      structure or even internal dynamics of the protein. As
                      larger domains contribute to the configurational changes,
                      the timescale of the involved motions is slowed down. The
                      role of slow domain dynamics is being increasingly
                      recognized as essential to understanding the function of
                      proteins. Neutron spin echo spectroscopy (NSE) is a
                      technique that is able to access the related timescales from
                      0.1 up to several hundred nanoseconds and simultaneously
                      covers the length scale relevant for protein domain
                      movements of several nanometers distance between domains.
                      Here we focus on these large-scale domain fluctuations and
                      show how the structure and dynamics of proteins can be
                      assessed by small-angle neutron scattering and NSE.},
      cin          = {ICS-1 / Neutronenstreuung ; JCNS-1},
      ddc          = {530},
      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:000345461700004},
      doi          = {10.1088/0953-8984/26/50/503103},
      url          = {https://juser.fz-juelich.de/record/187631},
}