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@ARTICLE{Feuerstein:16572,
      author       = {Feuerstein, S. and Solyom, Z. and Aladag, A. and Hoffmann,
                      S. and Willbold, D. and Brutscher, B.},
      title        = {1{H}, 13{C}, and 15{N}resonance assignment of a 179 residue
                      fragment of hepatitis {C} virus non-structural protein 5{A}},
      journal      = {Biomolecular NMR assignments},
      volume       = {5},
      issn         = {1874-2718},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Netherlands},
      reportid     = {PreJuSER-16572},
      pages        = {241 - 243},
      year         = {2011},
      note         = {This work was supported by the CEA, the CNRS, the
                      University of Grenoble 1, and the Deutsche
                      Forschungsgemeinschaft (SFB575). We would like to thank
                      Beate Bersch and Adrien Favier (IBS Grenoble) for
                      stimulating discussions.},
      abstract     = {Non-structural protein 5A (NS5A) plays an important role in
                      the life cycle of hepatitis C virus. This proline-rich
                      phosphoprotein is organized into three domains. Besides its
                      role in virus replication and virus assembly, NS5A is
                      involved in a variety of cellular regulation processes.
                      Recent studies on domain 2 and 3 revealed that both belong
                      to the class of intrinsically disordered proteins as they
                      adopt a natively unfolded state. In particular, domain 2
                      together with its vicinal regions is responsible for NS5A's
                      multiple interactions with other proteins necessary for
                      virus persistence. The low chemical shift dispersion
                      observed for instrinsically disordered proteins presents a
                      challenge for NMR spectroscopy. Here we report sequential
                      resonance assignment of a 179-residue fragment of NS5A,
                      comprising the entire domain 2, using a set of sensitivity
                      and resolution optimized 3D correlation experiments, as well
                      as amino-acid-type editing in (1)H-(15)N correlation
                      spectra. Our assignment reveals the presence of several
                      segments with high propensity to form α-helical structure
                      that may be of importance to the function of this protein
                      fragment as a versatile interaction platform.},
      keywords     = {Binding Sites / Hepacivirus: chemistry / Isotopes:
                      chemistry / Nuclear Magnetic Resonance, Biomolecular /
                      Protein Conformation / Protein Structure, Tertiary /
                      Recombinant Proteins: chemistry / Viral Nonstructural
                      Proteins: chemistry / Isotopes (NLM Chemicals) / NS-5
                      protein, hepatitis C virus (NLM Chemicals) / Recombinant
                      Proteins (NLM Chemicals) / Viral Nonstructural Proteins (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    = {Biophysics / Spectroscopy},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21516467},
      UT           = {WOS:000294559700027},
      doi          = {10.1007/s12104-011-9309-2},
      url          = {https://juser.fz-juelich.de/record/16572},
}