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@ARTICLE{Gardiennet:275,
      author       = {Gardiennet, C. and Loquet, A. and Bockmann, A and Etzkorn,
                      M. and Heise, H. and Baldus, M.},
      title        = {{S}tructural constraints for the {C}rh protein from
                      solid-state {NMR} experiments},
      journal      = {Journal of biomolecular NMR},
      volume       = {40},
      issn         = {0925-2738},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Science + Business Media B.V},
      reportid     = {PreJuSER-275},
      pages        = {239 - 250},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {We demonstrate that short, medium and long-range
                      constraints can be extracted from proton mediated, rare-spin
                      detected correlation solid-state NMR experiments for the
                      microcrystalline 10.4 x 2 kDa dimeric model protein Crh.
                      Magnetization build-up curves from cross signals in NHHC and
                      CHHC spectra deliver detailed information on side chain
                      conformers and secondary structure for interactions between
                      spin pairs. A large number of medium and long-range
                      correlations can be observed in the spectra, and an analysis
                      of the resolved signals reveals that the constraints cover
                      the entire sequence, also including inter-monomer contacts
                      between the two molecules forming the domain-swapped Crh
                      dimer. Dynamic behavior is shown to have an impact on cross
                      signals intensities, as indicated for mobile residues or
                      regions by contacts predicted from the crystal structure,
                      but absent in the spectra. Our work validates strategies
                      involving proton distance measurements for large and complex
                      proteins as the Crh dimer, and confirms the magnetization
                      transfer properties previously described for small molecules
                      in solid protein samples.},
      keywords     = {Bacterial Proteins: chemistry / Dimerization / Models,
                      Molecular / Nuclear Magnetic Resonance, Biomolecular:
                      methods / Phosphoproteins: chemistry / Protein Conformation
                      / Protons / Bacterial Proteins (NLM Chemicals) / Crh
                      protein, Bacillus subtilis (NLM Chemicals) / Phosphoproteins
                      (NLM Chemicals) / Protons (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    = {Biochemistry $\&$ Molecular Biology / Spectroscopy},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18320329},
      pmc          = {pmc:PMC2579321},
      UT           = {WOS:000254804800002},
      doi          = {10.1007/s10858-008-9229-3},
      url          = {https://juser.fz-juelich.de/record/275},
}