% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Do:139786,
      author       = {Do, Quynh Hoa and Wittlich, Marc and Glück, Julian and
                      Möckel, Luis and Willbold, Dieter and König, Bernd and
                      Heise, Henrike},
      title        = {{F}ull-length {V}pu and human {CD}4(372–433) in
                      phospholipid bilayers as seen by magic angle spinning {NMR}},
      journal      = {Biological chemistry},
      volume       = {394},
      number       = {11},
      issn         = {1437-4315},
      address      = {Berlin [u.a.]},
      publisher    = {de Gruyter},
      reportid     = {FZJ-2013-05758},
      pages        = {1453 - 1463},
      year         = {2013},
      abstract     = {HIV-1 Vpu and CD4(372-433), a peptide comprising the
                      transmembrane and cytoplasmic domain of human CD4, were
                      recombinantly expressed in Escherichia coli, uniformly
                      labeled with 13C and 15N isotopes, and separately
                      reconstituted into phospholipid bilayers. Highly resolved
                      dipolar cross-polarization (CP)-based solid-state NMR
                      spectra of the two transmembrane proteins were recorded
                      under magic angle sample spinning. Partial assignment of 13C
                      resonances was achieved. Site-specific assignments were
                      obtained for 13 amino acid residues of CD4(372-433) and two
                      Vpu residues. Additional amino acid type-specific
                      assignments were achieved for 10 amino acid spin systems for
                      both CD4(372-433) and Vpu. Further, structural flexibility
                      was probed with different dipolar recoupling techniques, and
                      the correct insertion of the transmembrane domains into the
                      lipid bilayers was confirmed by proton spin diffusion
                      experiments.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000325717100009},
      doi          = {10.1515/hsz-2013-0194},
      url          = {https://juser.fz-juelich.de/record/139786},
}