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@ARTICLE{Glck:7145,
      author       = {Glück, J.M. and Wittlich, M. and Feuerstein, S.E. and
                      Hoffmann, S. and Willbold, D. and Koenig, B. W.},
      title        = {{I}ntegral membrane proteins in nanodiscs can be studied by
                      solution {NMR} spectroscopy},
      journal      = {Journal of the American Chemical Society},
      volume       = {131},
      issn         = {0002-7863},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-7145},
      pages        = {12060 - 12061},
      year         = {2009},
      note         = {We thank Matthias Stoldt and Rudolf Hartmann for expert
                      assistance and discussions. This work was supported by a
                      grant from the Helmholtz Society ("Virtual Institute for
                      Structural Biology") to D.W.},
      abstract     = {We present a two-dimensional solution NMR spectrum of an
                      integral membrane protein (IMP) in a nanodisc. Solution NMR
                      relies on rapid isotropic tumbling of the analyte with
                      correlation times in the nanosecond range. IMPs in a
                      cellular membrane do not satisfy this condition. Previous
                      liquid-state NMR studies on IMPs were conducted in organic
                      solvent or artificial membrane mimicking particles like
                      detergent micelles. Nanodiscs are relatively small (150
                      kDa), detergent-free model membranes that are suitable for
                      functional reconstitution of IMPs. Nanodiscs allow
                      solubilization of integral membrane proteins in a nearly
                      native lipid bilayer environment. The 70 residue polypeptide
                      CD4mut was incorporated into nanodiscs. CD4mut features one
                      transmembrane helix. The aliphatic (1)H-(13)C HSQC spectrum
                      of nanodiscs with inserted, ((13)C, (15)N)-labeled CD4mut
                      exhibits reasonably dispersed protein and lipid NMR signals.
                      Our results demonstrate that IMPs in nanodiscs are amenable
                      to liquid-state NMR methodology.},
      keywords     = {Antigens, CD4: chemistry / Antigens, CD4: genetics / Humans
                      / Magnetic Resonance Spectroscopy / Membrane Proteins:
                      chemistry / Membrane Proteins: genetics / Membranes,
                      Artificial / Nanostructures: chemistry / Solutions /
                      Antigens, CD4 (NLM Chemicals) / Membrane Proteins (NLM
                      Chemicals) / Membranes, Artificial (NLM Chemicals) /
                      Solutions (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-3 / JARA-HPC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Chemistry, Multidisciplinary},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19663495},
      UT           = {WOS:000269379600020},
      doi          = {10.1021/ja904897p},
      url          = {https://juser.fz-juelich.de/record/7145},
}