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@ARTICLE{Ahlawat:1032080,
      author       = {Ahlawat, Sahil and Mote, Kaustubh R. and Lakomek,
                      Nils-Alexander and Agarwal, Vipin},
      title        = {{S}olid-{S}tate {NMR}: {M}ethods for {B}iological {S}olids},
      journal      = {Chemical reviews},
      volume       = {122},
      number       = {10},
      issn         = {0009-2665},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2024-05983},
      pages        = {9643 - 9737},
      year         = {2022},
      abstract     = {In the last two decades, solid-state nuclear magnetic
                      resonance (ssNMR) spectroscopy has transformed from a
                      spectroscopic technique investigating small molecules and
                      industrial polymers to a potent tool decrypting structure
                      and underlying dynamics of complex biological systems, such
                      as membrane proteins, fibrils, and assemblies, in
                      near-physiological environments and temperatures. This
                      transformation can be ascribed to improvements in hardware
                      design, sample preparation, pulsed methods, isotope labeling
                      strategies, resolution, and sensitivity. The fundamental
                      engagement between nuclear spins and radio-frequency pulses
                      in the presence of a strong static magnetic field is
                      identical between solution and ssNMR, but the experimental
                      procedures vastly differ because of the absence of molecular
                      tumbling in solids. This review discusses routinely employed
                      state-of-the-art static and MAS pulsed NMR methods relevant
                      for biological samples with rotational correlation times
                      exceeding 100’s of nanoseconds. Recent developments in
                      signal filtering approaches, proton methodologies, and
                      multiple acquisition techniques to boost sensitivity and
                      speed up data acquisition at fast MAS are also discussed.
                      Several examples of protein structures (globular, membrane,
                      fibrils, and assemblies) solved with ssNMR spectroscopy have
                      been considered. We also discuss integrated approaches to
                      structurally characterize challenging biological systems and
                      some newly emanating subdisciplines in ssNMR spectroscopy.},
      cin          = {IBI-7},
      ddc          = {540},
      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       = {35238547},
      UT           = {WOS:000823422100001},
      doi          = {10.1021/acs.chemrev.1c00852},
      url          = {https://juser.fz-juelich.de/record/1032080},
}