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@ARTICLE{Bronder:823850,
      author       = {Bronder, Anna M. and Bieker, Adeline and Elter, Shantha
                      and Etzkorn, Manuel and Häussinger, Dieter and Oesterhelt,
                      Filipp},
      title        = {{O}riented {M}embrane {P}rotein {R}econstitution into
                      {T}ethered {L}ipid {M}embranes for {AFM} {F}orce
                      {S}pectroscopy},
      journal      = {Biophysical journal},
      volume       = {111},
      number       = {9},
      issn         = {0006-3495},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {FZJ-2016-06490},
      pages        = {1925 - 1934},
      year         = {2016},
      abstract     = {Membrane proteins act as a central interface between the
                      extracellular environment and the intracellular response and
                      as such represent one of the most important classes of drug
                      targets. The characterization of the molecular properties of
                      integral membrane proteins, such as topology and interdomain
                      interaction, is key to a fundamental understanding of their
                      function. Atomic force microscopy (AFM) and force
                      spectroscopy have the intrinsic capabilities of
                      investigating these properties in a near-native setting.
                      However, atomic force spectroscopy of membrane proteins is
                      traditionally carried out in a crystalline setup.
                      Alternatively, model membrane systems, such as tethered
                      bilayer membranes, have been developed for surface-dependent
                      techniques. While these setups can provide a more native
                      environment, data analysis may be complicated by the
                      normally found statistical orientation of the reconstituted
                      protein in the model membrane. We have developed a model
                      membrane system that enables the study of membrane proteins
                      in a defined orientation by single-molecule force
                      spectroscopy. Our approach is demonstrated using cell-free
                      expressed bacteriorhodopsin coupled to a quartz glass
                      surface in a defined orientation through a protein anchor
                      and reconstituted inside an artificial membrane system. This
                      approach offers an effective way to study membrane proteins
                      in a planar lipid bilayer. It can be easily transferred to
                      all membrane proteins that possess a suitable tag and can be
                      reconstituted into a lipid bilayer. In this respect, we
                      anticipate that this technique may contribute important
                      information on structure, topology, and intra- and
                      intermolecular interactions of other seven-transmembrane
                      helical receptors.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000386594800014},
      pubmed       = {pmid:27806274},
      doi          = {10.1016/j.bpj.2016.08.051},
      url          = {https://juser.fz-juelich.de/record/823850},
}