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@ARTICLE{DeSantis:631439,
      author       = {De Santis, Emiliano and Mandl, Thomas and Kung, Jocky C. K.
                      and Huynh, Khon and Daly, Steven and D'Alessandro, Lorenza
                      A. and MacAleese, Luke and Uetrecht, Charlotte and Marklund,
                      Erik G. and Caleman, Carl},
      title        = {{S}tructural stability of chromophore-grafted {U}biquitin
                      mutants in vacuum},
      journal      = {Physical chemistry, chemical physics},
      volume       = {27},
      number       = {28},
      issn         = {1463-9076},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {PUBDB-2025-01951},
      pages        = {14767 - 14776},
      year         = {2025},
      abstract     = {Structural biology is witnessing a transformative era with
                      gas-phase techniques such as native mass spectrometry (MS),
                      ion mobility, and single-particle imaging (SPI) emerging as
                      critical tools for studying biomolecular assemblies like
                      protein capsids in their native states. SPI with X-ray
                      free-electron lasers has the potential to allow for
                      capturing atomic-resolution structures of proteins without
                      crystallization. However, determining particle orientation
                      during exposure remains a major challenge, compounded by the
                      heterogeneity of the protein complexes. Gas-phase Förster
                      resonance energy transfer (FRET) offers a promising solution
                      to assess alignment-induced structural perturbations,
                      providing insights into the stability of the tertiary
                      structure under various activation methods. This study
                      employs molecular dynamics (MD) simulations to explore
                      chromophore integration's effect on ubiquitin's structure
                      and alignment properties in vacuum. Ubiquitin serves as an
                      ideal model due to its small size, well-characterized
                      properties, and computational simplicity. By investigating
                      chromophore placement, we identified optimal sites for
                      monitoring gas-phase denaturation and unfolding processes,
                      advancing SPI applications and a broader understanding of
                      protein stability in the gas phase.},
      cin          = {CSSB-LIV/DESY-CU},
      ddc          = {540},
      cid          = {$I:(DE-H253)CSSB-LIV_DESY-CU-20220525$},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40464121},
      doi          = {10.1039/D5CP01297J},
      url          = {https://bib-pubdb1.desy.de/record/631439},
}