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@ARTICLE{Stief:1014224,
      author       = {Stief, Tobias and Gremer, Lothar and Pribicevic, Sonja and
                      Espinueva, Delane F. and Vormann, Katharina and Biehl, Ralf
                      and Jahn, Reinhard and Pérez-Lara, Ángel and Lakomek,
                      Nils},
      title        = {{I}ntrinsic {D}isorder of the {N}euronal {SNARE} {P}rotein
                      {SNAP}25a in its {P}re-fusion {C}onformation},
      journal      = {Journal of molecular biology},
      volume       = {435},
      number       = {10},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2023-03208},
      pages        = {168069 -},
      year         = {2023},
      abstract     = {The neuronal SNARE protein SNAP25a (isoform 2) forms part
                      of the SNARE complex eliciting synaptic vesicle fusion
                      during neuronal exocytosis. While the post-fusion cis-SNARE
                      complex has been studied extensively, little is known about
                      the pre-fusion conformation of SNAP25a. Here we analyze
                      monomeric SNAP25a by NMR spectroscopy, further supported by
                      small-angle X-ray scattering (SAXS) experiments. SAXS data
                      indicate that monomeric SNAP25 is more compact than a
                      Gaussian chain but still a random coil. NMR shows that for
                      monomeric SNAP25a, before SNAP25a interacts with its SNARE
                      partners to drive membrane fusion, only the N-terminal part
                      (region A5 to V36) of the first SNARE motif, SN1 (L11 -
                      L81), is helical, comprising two α-helices (ranging from A5
                      to Q20 and S25 toV36). From E37 onwards, SNAP25a is mostly
                      disordered and displays high internal flexibility, including
                      the C-terminal part of SN1, almost the entire second SNARE
                      motif (SN2, N144-A199), and the connecting loop region.
                      Apart from the N-terminal helices, only the C-termini of
                      both SN1 (E73 - K79) and SN2 (region T190 - A199), as well
                      as two short regions in the connecting loop (D99 - K102 and
                      E123 - M127) show a weak α-helical propensity (α-helical
                      population < $25\%).$ We speculate that the N-terminal
                      helices (A5 to Q20 and S25 to V36) which constitute the
                      N-terminus of SN1 act as a nucleation site for initiating
                      SNARE zippering.},
      cin          = {JCNS-1 / IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)IBI-7-20200312},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ)
                      (POF4-6G4) / 633 - Life Sciences – Building Blocks of
                      Life: Structure and Function (POF4-633) / 5244 - Information
                      Processing in Neuronal Networks (POF4-524)},
      pid          = {G:(DE-HGF)POF4-6G4 / G:(DE-HGF)POF4-633 /
                      G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37003471},
      UT           = {WOS:001030007700001},
      doi          = {10.1016/j.jmb.2023.168069},
      url          = {https://juser.fz-juelich.de/record/1014224},
}