% 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{Michalczyk:276225,
      author       = {Michalczyk, Ryszard and Unkefer, Clifford J. and Bacik,
                      John-Paul and Schrader, Tobias E. and Ostermann, Andreas and
                      Kovalevsky, Andrey Y. and McKenna, Robert and Fisher,
                      Suzanne Zoë},
      title        = {{J}oint neutron crystallographic and {NMR} solution studies
                      of {T}yr residue ionization and hydrogen bonding:
                      {I}mplications for enzyme-mediated proton transfer},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {112},
      number       = {18},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2015-06690},
      pages        = {5673 - 5678},
      year         = {2015},
      abstract     = {Proton transfer is a fundamental mechanism at the core of
                      many enzyme-catalyzed reactions. It is also exquisitely
                      sensitive to a number of factors, including pH,
                      electrostatics, proper active-site geometry, and chemistry.
                      Carbonic anhydrase has evolved a fast and efficient way to
                      conduct protons through a combination of hydrophilic amino
                      acid side chains that coordinate a highly ordered H-bonded
                      water network. This study uses a powerful approach,
                      combining NMR solution studies with neutron protein
                      crystallography, to determine the effect of pH and divalent
                      cations on key residues involved in proton transfer in human
                      carbonic anhydrase. The results have broad implications for
                      our understanding of proton transfer and how subtle changes
                      in ionization and H-bonding interactions can modulate enzyme
                      catalysis.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {000},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000353953800049},
      doi          = {10.1073/pnas.1502255112},
      url          = {https://juser.fz-juelich.de/record/276225},
}