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@ARTICLE{Uluca:844352,
      author       = {Uluca, Boran and Viennet, Thibault and Petrović, Dušan
                      and Shaykhalishahi, Hamed and Weirich, Franziska and
                      Gönülalan, Ayşenur and Strodel, Birgit and Etzkorn,
                      Manuel and Hoyer, Wolfgang and Heise, Henrike},
      title        = {{DNP}-{E}nhanced {MAS} {NMR}: {A} {T}ool to {S}napshot
                      {C}onformational {E}nsembles of α -{S}ynuclein in
                      {D}ifferent {S}tates},
      journal      = {Biophysical journal},
      volume       = {114},
      number       = {7},
      issn         = {0006-3495},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {FZJ-2018-01783},
      pages        = {1614 - 1623},
      year         = {2018},
      abstract     = {Intrinsically disordered proteins dynamically sample a wide
                      conformational space and therefore do not adopt a stable and
                      defined three-dimensional conformation. The structural
                      heterogeneity is related to their proper functioning in
                      physiological processes. Knowledge of the conformational
                      ensemble is crucial for a complete comprehension of this
                      kind of proteins. We here present an approach that utilizes
                      dynamic nuclear polarization-enhanced solid-state NMR
                      spectroscopy of sparsely isotope-labeled proteins in frozen
                      solution to take snapshots of the complete structural
                      ensembles by exploiting the inhomogeneously broadened
                      line-shapes. We investigated the intrinsically disordered
                      protein α-synuclein (α-syn), which plays a key role in the
                      etiology of Parkinson’s disease, in three different
                      physiologically relevant states. For the free monomer in
                      frozen solution we could see that the so-called “random
                      coil conformation” consists of α-helical and
                      β-sheet-like conformations, and that secondary chemical
                      shifts of neighboring amino acids tend to be correlated,
                      indicative of frequent formation of secondary structure
                      elements. Based on these results, we could estimate the
                      number of disordered regions in fibrillar α-syn as well as
                      in α-syn bound to membranes in different protein-to-lipid
                      ratios. Our approach thus provides quantitative information
                      on the propensity to sample transient secondary structures
                      in different functional states. Molecular dynamics
                      simulations rationalize the results.},
      cin          = {ICS-6 / JARA-HPC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / $I:(DE-82)080012_20140620$},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      Computational Enzyme Design $(jics69_20151101)$},
      pid          = {G:(DE-HGF)POF3-551 / $G:(DE-Juel1)jics69_20151101$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29642031},
      UT           = {WOS:000430214500011},
      doi          = {10.1016/j.bpj.2018.02.011},
      url          = {https://juser.fz-juelich.de/record/844352},
}