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@ARTICLE{Varga:626436,
      author       = {Varga, Soma and Péterfia, Bálint Ferenc and Dudola,
                      Dániel and Farkas, Viktor and Jeffries, Cy M. and Permi,
                      Perttu and Gáspári, Zoltán},
      title        = {{D}ynamic {I}nterchange of {L}ocal {R}esidue-{R}esidue
                      {I}nteractions in the {L}argely {E}xtended {S}ingle
                      {A}lpha-{H}elix in {D}rebrin},
      journal      = {Biochemical journal},
      volume       = {482},
      number       = {08},
      issn         = {0006-2936},
      address      = {London},
      publisher    = {Portland Press},
      reportid     = {PUBDB-2025-01415},
      pages        = {383 - 399},
      year         = {2025},
      note         = {ISSN 1470-8728 not unique: **2 hits**.},
      abstract     = {Single alpha-helices (SAHs) are protein regions with unique
                      mechanical properties, forming long stable monomeric helical
                      structures in solution. To date, only a few naturally
                      occurring SAH regions have been extensively characterized,
                      primarily from myosins, leaving the structural and dynamic
                      variability of SAH regions largely unexplored. Drebrin
                      (developmentally regulated brain protein) contains a
                      predicted SAH segment with unique sequence characteristics,
                      including aromatic residues within the SAH region and a
                      preference for arginine over lysine in its C-terminal half.
                      Using and NMR spectroscopy, combined with SAXS measurements,
                      we demonstrate that the Drebrin-SAH is helical and monomeric
                      in solution. NMR resonance assignment required specific 4D
                      techniques to resolve severe signal overlap resulting from
                      the low complexity and largely helical conformation of the
                      sequence. To further characterize its structure, we
                      generated a structural ensemble consistent with Cα, Cβ
                      chemical shifts and SAXS data, revealing a primarily
                      extended structure with non-uniform helicity. Our results
                      suggest that dynamic rearrangement of salt bridges and
                      potential transient cation-π interactions contribute to the
                      formation and stabilization of both helical and non-helical
                      local conformational states.},
      cin          = {EMBL-User / EMBL},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {40192062},
      UT           = {WOS:001489807200002},
      doi          = {10.1042/BCJ20253036},
      url          = {https://bib-pubdb1.desy.de/record/626436},
}