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@ARTICLE{Lazaratos:943341,
      author       = {Lazaratos, Michalis and Siemers, Malte and Brown, Leonid S.
                      and Bondar, Ana-Nicoleta},
      title        = {{C}onserved hydrogen-bond motifs of membrane transporters
                      and receptors},
      journal      = {Biochimica et biophysica acta / Biomembranes},
      volume       = {1864},
      number       = {6},
      issn         = {0005-2728},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {FZJ-2023-00947},
      pages        = {183896 -},
      year         = {2022},
      abstract     = {Membrane transporters and receptors often rely on conserved
                      hydrogen bonds to assemble transient paths for ion transfer
                      or long-distance conformational couplings. For transporters
                      and receptors that use proton binding and proton transfer
                      for function, inter-helical hydrogen bonds of titratable
                      protein sidechains that could change protonation are of
                      central interest to formulate hypotheses about reaction
                      mechanisms. Knowledge of hydrogen bonds common at sites of
                      potential interest for proton binding could thus inform and
                      guide studies on functional mechanisms of
                      protonation-coupled membrane proteins. Here we apply
                      graph-theory approaches to identify hydrogen-bond motifs of
                      carboxylate and histidine sidechains in a large data set of
                      static membrane protein structures. We find that
                      carboxylate-hydroxyl hydrogen bonds are present in numerous
                      structures of the dataset, and can be part of more extended
                      H-bond clusters that could be relevant to conformational
                      coupling. Carboxylate-carboxyamide and imidazole-imidazole
                      hydrogen bonds are represented in comparably fewer protein
                      structures of the dataset. Atomistic simulations on two
                      membrane transporters in lipid membranes suggest that many
                      of the hydrogen bond motifs present in static protein
                      structures tend to be robust, and can be part of larger
                      hydrogen-bond clusters that recruit additional hydrogen
                      bonds.},
      cin          = {IAS-5 / INM-9},
      ddc          = {570},
      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       = {35217000},
      UT           = {WOS:000788122400005},
      doi          = {10.1016/j.bbamem.2022.183896},
      url          = {https://juser.fz-juelich.de/record/943341},
}