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@ARTICLE{Feuerstein:19969,
      author       = {Feuerstein, S. and Plevin, M.J. and Willbold, D. and
                      Brutscher, B.},
      title        = {i{HADAMAC}: a complementary tool for sequential resonance
                      assignment of globular and highly disordered protein},
      journal      = {Journal of magnetic resonance},
      volume       = {214},
      issn         = {1090-7807},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-19969},
      pages        = {329 - 334},
      year         = {2012},
      note         = {We thank I. Ayala (IBS Grenoble) for help with the
                      production of the protein samples used for this study, and
                      S. Hoffmann (FZ Julich) for stimulating discussion on the
                      NS5A project. This work has been supported in part by grants
                      from the European Commission (FP7-I3-BIO-NMR contract No.
                      261862, FP7-ITN-IDPbyNMR contract No. 264257, and
                      FPR-IRG-2008 contract No. 231082), and financial support
                      from ARC to M.J.P. and from CEA to S.F.},
      abstract     = {An experiment, iHADAMAC, is presented that yields
                      information on the amino-acid type of individual residues in
                      a protein by editing the (1)H-(15)N correlations into seven
                      different 2D spectra, each corresponding to a different
                      class of amino-acid types. Amino-acid type discrimination is
                      realized via a Hadamard encoding scheme based on four
                      different spin manipulations as recently introduced in the
                      context of the sequential HADAMAC experiment. Both
                      sequential and intra-residue HADAMAC experiments yield
                      highly complementary information that greatly facilitate
                      resonance assignment of proteins with high frequency
                      degeneracy, as demonstrated here for a 188-residue
                      intrinsically disordered protein fragment of the hepatitis C
                      virus protein NS5A.},
      keywords     = {Algorithms / Magnetic Resonance Spectroscopy: methods /
                      Proteins: chemistry / Proteins: ultrastructure / Software /
                      Proteins (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {550},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung / IDPBYNMR - High resolution tools
                      to understand the functional role of protein intrinsic
                      disorder (264257) / ONCOMIRNA-BIOGENESIS - Biogenesis of
                      Oncogenic MicroRNAs : from the structure of the microRNA
                      processing complexes to the inhibition of the maturation of
                      human oncogenes (231082)},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505 /
                      G:(EU-Grant)264257 / G:(EU-Grant)231082},
      shelfmark    = {Biochemical Research Methods / Physics, Atomic, Molecular
                      $\&$ Chemical / Spectroscopy},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22123230},
      UT           = {WOS:000299656400043},
      doi          = {10.1016/j.jmr.2011.10.019},
      url          = {https://juser.fz-juelich.de/record/19969},
}