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@ARTICLE{Glck:11819,
      author       = {Glück, J.M. and Koenig, B. W. and Willbold, D.},
      title        = {{N}anodiscs allow the use of integral membrane proteins as
                      analytes in surface plasmon resonance studies},
      journal      = {Analytical biochemistry},
      volume       = {408},
      issn         = {0003-2697},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-11819},
      pages        = {46 - 52},
      year         = {2011},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Nanodiscs are small-sized and flat model membranes that
                      provide a close to native environment for reconstitution of
                      integral membrane proteins. Incorporation of membrane
                      proteins into nanodiscs results in water-soluble proteolipid
                      particles making the membrane proteins amenable to a
                      multitude of bioanalytical techniques originally developed
                      for soluble proteins. The transmembrane domain of the human
                      CD4 receptor was fused to ubiquitin with a preceding
                      N-terminal decahistidine tag. The resulting integral
                      membrane protein was incorporated into nanodiscs. Binding of
                      the nanodisc-inserted histidine-tagged protein to a
                      monoclonal anti-pentahistidine antibody was quantified using
                      surface plasmon resonance (SPR) experiments. For the first
                      time, a membrane-inserted transmembrane protein was employed
                      as analyte while the antibody served as ligand immobilized
                      on the sensor chip surface. SPR experiments were conducted
                      in single-cycle mode. We demonstrate that the
                      nanodisc-incorporated membrane protein showed nearly
                      identical affinity toward the antibody as did the soluble
                      decahistidine-tagged ubiquitin studied in a comparative
                      experiment. Advantages of the new experimental setup and
                      potential applications are discussed.},
      keywords     = {Antibodies, Monoclonal: immunology / Antigens, CD4:
                      chemistry / Antigens, CD4: genetics / Antigens, CD4:
                      metabolism / Biosensing Techniques: methods / Humans /
                      Kinetics / Membrane Proteins: chemistry / Membrane Proteins:
                      genetics / Membrane Proteins: metabolism / Nanostructures:
                      chemistry / Oligopeptides: chemistry / Oligopeptides:
                      genetics / Oligopeptides: metabolism / Protein Binding /
                      Recombinant Fusion Proteins: chemistry / Recombinant Fusion
                      Proteins: genetics / Recombinant Fusion Proteins: metabolism
                      / Surface Plasmon Resonance: methods / Ubiquitin: chemistry
                      / Ubiquitin: genetics / Ubiquitin: metabolism / Antibodies,
                      Monoclonal (NLM Chemicals) / Antigens, CD4 (NLM Chemicals) /
                      Membrane Proteins (NLM Chemicals) / Oligopeptides (NLM
                      Chemicals) / Recombinant Fusion Proteins (NLM Chemicals) /
                      Ubiquitin (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemical Research Methods / Biochemistry $\&$ Molecular
                      Biology / Chemistry, Analytical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20804721},
      UT           = {WOS:000283886600007},
      doi          = {10.1016/j.ab.2010.08.028},
      url          = {https://juser.fz-juelich.de/record/11819},
}