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@ARTICLE{Lakomek:1031670,
      author       = {Lakomek, Nils and Stief, Tobias and Vormann, Katharina},
      title        = {{NMR} 15{N} {R}elaxation {E}xperiments for the
                      {I}nvestigation of {P}icosecond to {N}anoseconds
                      {S}tructural {D}ynamics of {P}roteins},
      journal      = {JoVE journal},
      volume       = {},
      issn         = {1940-087X},
      address      = {Cambridge, MA},
      publisher    = {JoVE},
      reportid     = {FZJ-2024-05780},
      pages        = {e67088},
      year         = {2024},
      abstract     = {Nuclear magnetic resonance (NMR) spectroscopy allows
                      studying proteins in solution and under physiological
                      temperatures. Frequently, either the amide groups of the
                      protein backbone or the methyl groups in side chains are
                      used as reporters of structural dynamics in proteins. A
                      structural dynamics study of the protein backbone of
                      globular proteins on 15N labeled and fully protonated
                      samples usually works well for proteins with a molecular
                      weight of up to 50 kDa. When side chain deuteration in
                      combination with transverse relaxation optimized
                      spectroscopy (TROSY) is applied, this limit can be extended
                      up to 200 kDa for globular proteins and up to 1 MDa when the
                      focus is on the side chains. When intrinsically disordered
                      proteins (IDPs) or proteins with intrinsically disordered
                      regions (IDRs) are investigated, these weight limitations do
                      not apply but can go well beyond. The reason is that IDPs or
                      IDRs, characterized by high internal flexibility, are
                      frequently dynamically decoupled. Various NMR methods offer
                      atomic-resolution insights into structural protein dynamics
                      across a wide range of time scales, from picoseconds up to
                      hours. Standard 15N relaxation measurements overview a
                      protein's internal flexibility and characterize the protein
                      backbone dynamics experienced on the fast pico- to
                      nanosecond timescale. This article presents a hands-on
                      protocol for setting up and recording NMR 15N R1, R2, and
                      heteronuclear Overhauser effect (hetNOE) experiments. We
                      show exemplary data and explain how to interpret them simply
                      qualitatively before any more sophisticated analysis.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {39555784},
      UT           = {WOS:001368152600029},
      doi          = {10.3791/67088},
      url          = {https://juser.fz-juelich.de/record/1031670},
}