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@ARTICLE{Gie:41694,
      author       = {Gieß, F. and Friedrich, M. and Heberle, J. and Naumann, R.
                      and Knoll, W.},
      title        = {{T}he {P}rotein {T}ethered {L}ipid {B}ilayer - a novel
                      mimic of the biological membrane},
      journal      = {Biophysical journal},
      volume       = {87},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-41694},
      pages        = {3213 - 3220},
      year         = {2004},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {A new concept of solid-supported tethered bilayer lipid
                      membrane (tBLM) for the functional incorporation of membrane
                      proteins is introduced. The incorporated protein itself acts
                      as the tethering molecule resulting in a versatile system in
                      which the protein determines the characteristics of the
                      submembraneous space. This architecture is achieved through
                      a metal chelating surface, to which histidine-tagged
                      (His-tagged) membrane proteins are able to bind in a
                      reversible manner. The tethered bilayer lipid membrane is
                      generated by substitution of protein-bound detergent
                      molecules with lipids using in-situ dialysis or adsorption.
                      The system is characterized by surface plasmon resonance,
                      quartz crystal microbalance, and electrochemical impedance
                      spectroscopy. His-tagged cytochrome c oxidase (CcO) is used
                      as a model protein in this study. However, the new system
                      should be applicable to all recombinant membrane proteins
                      bearing a terminal His-tag. In particular, combination of
                      surface immobilization and membrane reconstitution opens new
                      prospects for the investigation of functional membrane
                      proteins by various surface-sensitive techniques under a
                      defined electric field.},
      keywords     = {Biomimetics: methods / Cell Membrane: chemistry / Electric
                      Impedance / Electron Transport Complex IV: chemistry /
                      Histidine: chemistry / Lipid Bilayers: chemistry /
                      Macromolecular Substances / Membrane Fluidity / Membrane
                      Proteins: chemistry / Membranes, Artificial / Molecular
                      Conformation / Protein Binding / Lipid Bilayers (NLM
                      Chemicals) / Macromolecular Substances (NLM Chemicals) /
                      Membrane Proteins (NLM Chemicals) / Membranes, Artificial
                      (NLM Chemicals) / Histidine (NLM Chemicals) / Electron
                      Transport Complex IV (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15339795},
      pmc          = {pmc:PMC1304791},
      UT           = {WOS:000224732500026},
      doi          = {10.1529/biophysj.104.046169},
      url          = {https://juser.fz-juelich.de/record/41694},
}