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@ARTICLE{Varghese:140004,
      author       = {Varghese, Sabu and Yang, Fei and Pacheco, Victor and Wrede,
                      Kathrin and Medvedev, Alexander and Ogata, Hideaki and
                      Knipp, Markus and Heise, Henrike},
      title        = {{E}xpression, {P}urification, and {S}olid-{S}tate {NMR}
                      {C}haracterization of the {M}embrane {B}inding {H}eme
                      {P}rotein {N}itrophorin 7 in {T}wo {E}lectronic {S}pin
                      {S}tates},
      journal      = {Biochemistry},
      volume       = {52},
      number       = {40},
      issn         = {1520-4995},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2013-05971},
      pages        = {7031 - 7040},
      year         = {2013},
      abstract     = {The nitrophorins (NPs) comprise a group of NO transporting
                      ferriheme b proteins found in the saliva of the blood
                      sucking insect Rhodnius prolixus. In contrast to other
                      nitrophorins (NP1–4), the recently identified membrane
                      binding isoform NP7 tends to form oligomers and precipitates
                      at higher concentrations in solution. Hence, solid-state NMR
                      (ssNMR) was employed as an alternative method to gain
                      structural insights on the precipitated protein. We report
                      the expression and purification of 13C,15N isotopically
                      labeled protein together with the first ssNMR
                      characterization of NP7. Because the size of NP7 (21 kDa)
                      still provides a challenge for ssNMR, the samples were
                      reverse labeled with Lys and Val to reduce the number of
                      crosspeaks in two-dimensional spectra. The two electronic
                      spin states with S = 1/2 and S = 0 at the ferriheme iron
                      were generated by the complexation with imidazole and NO,
                      respectively. ssNMR spectra of both forms are well resolved,
                      which allows for sequential resonance assignments of 22
                      residues. Importantly, the ssNMR spectra demonstrate that
                      aggregation does not affect the protein fold. Comparison of
                      the spectra of the two electronic spin states allows the
                      determination of paramagnetically shifted cross peaks due to
                      pseudocontact shifts, which assists the assignment of
                      residues close to the heme center.},
      cin          = {ICS-6},
      ddc          = {570},
      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:000326355500011},
      pubmed       = {pmid:24033104},
      doi          = {10.1021/bi401020t},
      url          = {https://juser.fz-juelich.de/record/140004},
}