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@ARTICLE{Sanabria:874540,
      author       = {Sanabria, Hugo and Rodnin, Dmitro and Hemmen, Katherina and
                      Peulen, Thomas-Otavio and Felekyan, Suren and Fleissner,
                      Mark R. and Dimura, Mykola and Koberling, Felix and
                      Kühnemuth, Ralf and Hubbell, Wayne and Gohlke, Holger and
                      Seidel, Claus A. M.},
      title        = {{R}esolving dynamics and function of transient states in
                      single enzyme molecules},
      journal      = {Nature Communications},
      volume       = {11},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2020-01495},
      pages        = {1231},
      year         = {2020},
      abstract     = {We use a hybrid fluorescence spectroscopic toolkit to
                      monitor T4 Lysozyme (T4L) in action by unraveling the
                      kinetic and dynamic interplay of the conformational states.
                      In particular, by combining single-molecule and ensemble
                      multiparameter fluorescence detection, EPR spectroscopy,
                      mutagenesis, and FRET-positioning and screening, and other
                      biochemical and biophysical tools, we characterize three
                      short-lived conformational states over the ns-ms timescale.
                      The use of 33 FRET-derived distance sets, to screen
                      available T4L structures, reveal that T4L in solution mainly
                      adopts the known open and closed states in exchange at
                      4 µs. A newly found minor state, undisclosed by, at
                      present, more than 500 crystal structures of T4L and sampled
                      at 230 µs, may be actively involved in the product
                      release step in catalysis. The presented fluorescence
                      spectroscopic toolkit will likely accelerate the development
                      of dynamic structural biology by identifying transient
                      conformational states that are highly abundant in biology
                      and critical in enzymatic reactions.},
      cin          = {NIC / JSC / IBI-7},
      ddc          = {500},
      cid          = {I:(DE-Juel1)NIC-20090406 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)IBI-7-20200312},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511) / Forschergruppe Gohlke $(hkf7_20170501)$},
      pid          = {G:(DE-HGF)POF3-511 / $G:(DE-Juel1)hkf7_20170501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32144241},
      UT           = {WOS:000549162600008},
      doi          = {10.1038/s41467-020-14886-w},
      url          = {https://juser.fz-juelich.de/record/874540},
}