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@ARTICLE{Scheidt:59162,
      author       = {Scheidt, H. A. and Vogel, A. and Eckhoff, A. and Koenig, B.
                      W. and Huster, D.},
      title        = {{S}olid-state {NMR} characterization of the putative
                      membrane anchor of {TWD}1 from {A}rabidopsis thaliana},
      journal      = {European biophysics journal},
      volume       = {36},
      issn         = {0175-7571},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {PreJuSER-59162},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Structure and membrane interaction of a 31 amino acid
                      residue fragment of the membrane bound FKBP-like protein
                      twisted dwarf 1 (TWD1) from Arabidopsis thaliana was
                      investigated by solid-state NMR spectroscopy. The studied
                      peptide TWD1(335-365) contained the putative membrane anchor
                      of the protein (residues 339-357) that was previously
                      predicted by sequence hydrophobicity analysis. The TWD1
                      peptide was synthesized by standard solid phase peptide
                      synthesis and contained three uniformly (13)C- and
                      (15)N-labelled residues (Phe 340, Val 350, Ala 364). The
                      peptide was incorporated into either multilamellar vesicles
                      or oriented planar membranes composed of an equimolar
                      ternary phospholipid mixture (POPC, POPE, POPG), where the
                      POPC was sn-1 chain-deuterated. (31)P NMR spectra of the
                      membrane in the absence and in the presence of the peptide
                      showed axially symmetric powder patterns indicative of a
                      lamellar bilayer phase. Further, the addition of peptide
                      caused a decrease in the lipid hydrocarbon chain order as
                      indicated by reduced quadrupolar splittings in the (2)H NMR
                      spectra of the POPC in the membrane. The conformation of
                      TWD1(335-365) was investigated by (13)C cross-polarization
                      magic-angle spinning NMR spectroscopy. At a temperature of
                      -30 degrees C all peptide signals were resolved and could be
                      fully assigned in two-dimensional proton-driven (13)C spin
                      diffusion and (13)C single quantum/double quantum
                      correlation experiments. The isotropic chemical shift values
                      for Phe 340 and Val 350 exhibited the signature of a regular
                      alpha-helix. Chemical shifts typical for a random coil
                      conformation were observed for Ala 364 located close to the
                      C-terminus of the peptide. Static (15)N NMR spectra of
                      TWD1(335-365) in mechanically aligned lipid bilayers
                      demonstrated that the helical segment of TWD1(335-365)
                      adopts an orientation perpendicular to the membrane normal.
                      At 30 degrees C, the peptide undergoes intermediate time
                      scale motions.},
      keywords     = {Arabidopsis Proteins: chemistry / Binding Sites / Cell
                      Membrane: chemistry / Glycosylphosphatidylinositols:
                      chemistry / Lipid Bilayers: chemistry / Magnetic Resonance
                      Spectroscopy / Membrane Fusion / Protein Binding /
                      Tacrolimus Binding Proteins: chemistry / Arabidopsis
                      Proteins (NLM Chemicals) / Glycosylphosphatidylinositols
                      (NLM Chemicals) / Lipid Bilayers (NLM Chemicals) / TWD1
                      protein, Arabidopsis (NLM Chemicals) / Tacrolimus Binding
                      Proteins (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17033777},
      UT           = {WOS:000245826200014},
      doi          = {10.1007/s00249-006-0094-2},
      url          = {https://juser.fz-juelich.de/record/59162},
}