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@ARTICLE{Hermans:837232,
      author       = {Hermans, Susanne M. A. and Pfleger, Christopher and
                      Nutschel, Christina and Hanke, Christian A. and Gohlke,
                      Holger},
      title        = {{R}igidity theory for biomolecules: concepts, software, and
                      applications},
      journal      = {Wiley interdisciplinary reviews / Computational Molecular
                      Science},
      volume       = {7},
      number       = {4},
      issn         = {1759-0876},
      address      = {Malden, MA},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2017-06207},
      pages        = {e1311},
      year         = {2017},
      abstract     = {The mechanical heterogeneity of biomolecular structures is
                      intimately linked to their diverse biological functions.
                      Applying rigidity theory to biomolecules identifies this
                      heterogeneous composition of flexible and rigid regions,
                      which can aid in the understanding of biomolecular stability
                      and long-ranged information transfer through biomolecules,
                      and yield valuable information for rational drug design and
                      protein engineering. We review fundamental concepts in
                      rigidity theory, ways to represent biomolecules as
                      constraint networks, and methodological and algorithmic
                      developments for analyzing such networks and linking the
                      results to biomolecular function. Software packages for
                      performing rigidity analyses on biomolecules in an
                      efficient, automated way are described, as are rigidity
                      analyses on biomolecules including the ribosome, viruses, or
                      transmembrane proteins. The analyses address questions of
                      allosteric mechanisms, mutation effects on
                      (thermo-)stability, protein (un-)folding, and
                      coarse-graining of biomolecules. We advocate that the
                      application of rigidity theory to biomolecules has matured
                      in such a way that it could be broadly applied as a
                      computational biophysical method to scrutinize biomolecular
                      function from a structure-based point of view and to
                      complement approaches focused on biomolecular dynamics. We
                      discuss possibilities to improve constraint network
                      representations and to perform large-scale and prospective
                      studies. WIREs Comput Mol Sci 2017, 7:e1311. doi:
                      10.1002/wcms.1311},
      cin          = {ICS-6 / JSC},
      ddc          = {004},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)JSC-20090406},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000403439500004},
      doi          = {10.1002/wcms.1311},
      url          = {https://juser.fz-juelich.de/record/837232},
}