% 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{Bondar:943342,
      author       = {Bondar, Ana-Nicoleta},
      title        = {{G}raphs of {H}ydrogen-{B}ond {N}etworks to {D}issect
                      {P}rotein {C}onformational {D}ynamics},
      journal      = {The journal of physical chemistry / B},
      volume       = {126},
      number       = {22},
      issn         = {1520-6106},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2023-00948},
      pages        = {3973 - 3984},
      year         = {2022},
      abstract     = {Dynamic hydrogen bonds and hydrogen-bond networks are
                      ubiquitous in proteins and protein complexes. Functional
                      roles that have been assigned to hydrogen-bond networks
                      include structural plasticity for protein function,
                      allosteric conformational coupling, long-distance proton
                      transfers, and transient storage of protons. Advances in
                      structural biology provide invaluable insights into
                      architectures of large proteins and protein complexes of
                      direct interest to human physiology and disease, including G
                      Protein Coupled Receptors (GPCRs) and the SARS-Covid-19
                      spike protein S, and give rise to the challenge of how to
                      identify those interactions that are more likely to govern
                      protein dynamics. This Perspective discusses applications of
                      graph-based algorithms to dissect dynamical hydrogen-bond
                      networks of protein complexes, with illustrations for GPCRs
                      and spike protein S. H-bond graphs provide an overview of
                      sites in GPCR structures where hydrogen-bond dynamics would
                      be required to assemble longer-distance networks between
                      functionally important motifs. In the case of spike protein
                      S, graphs identify regions of the protein where hydrogen
                      bonds rearrange during the reaction cycle and where local
                      hydrogen-bond networks likely change in a virus variant of
                      concern.},
      cin          = {IAS-5 / INM-9},
      ddc          = {530},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35639610},
      UT           = {WOS:000810266500001},
      doi          = {10.1021/acs.jpcb.2c00200},
      url          = {https://juser.fz-juelich.de/record/943342},
}