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@ARTICLE{Stief:1025608,
      author       = {Stief, Tobias and Vormann, Katharina and Lakomek,
                      Nils-Alexander},
      title        = {{S}ensitivity-enhanced {NMR} 15{N} {R}1 and {R}1ρ
                      relaxation experiments for the investigation of
                      intrinsically disordered proteins at high magnetic fields},
      journal      = {Methods},
      volume       = {223},
      issn         = {1046-2023},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {FZJ-2024-03002},
      pages        = {1 - 15},
      year         = {2024},
      abstract     = {NMR relaxation experiments provide residue-specific
                      insights into the structural dynamics of proteins. Here, we
                      present an optimized set of sensitivity-enhanced 15N R1 and
                      R1ρ relaxation experiments applicable to fully protonated
                      proteins. The NMR pulse sequences are conceptually similar
                      to the set of TROSY-based sequences and their HSQC
                      counterpart (Lakomek et al., J. Biomol. NMR 2012). Instead
                      of the TROSY read-out scheme, a sensitivity-enhanced HSQC
                      read-out scheme is used, with improved and easier optimized
                      water suppression. The presented pulse sequences are applied
                      on the cytoplasmic domain of the SNARE protein
                      Synpatobrevin-2 (Syb-2), which is intrinsically disordered
                      in its monomeric pre-fusion state. A two-fold increase in
                      the obtained signal-to-noise ratio is observed for this
                      intrinsically disordered protein, therefore offering a
                      four-fold reduction of measurement time compared to the
                      TROSY-detected version. The inter-scan recovery delay can be
                      shortened to two seconds. Pulse sequences were tested at 600
                      MHz and 1200 MHz 1H Larmor frequency, thus applicable over a
                      wide magnetic field range. A comparison between protonated
                      and deuterated protein samples reveals high agreement,
                      indicating that reliable 15N R1 and R1ρ rate constants can
                      be extracted for fully protonated and deuterated samples.
                      The presented pulse sequences will benefit not only for IDPs
                      but also for an entire range of low and medium-sized
                      proteins.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {38242384},
      UT           = {WOS:001175269700001},
      doi          = {10.1016/j.ymeth.2024.01.008},
      url          = {https://juser.fz-juelich.de/record/1025608},
}