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@ARTICLE{Drner:456627,
      author       = {Dörner, Simon and Schwob, Lucas and Schubert, Kaja and
                      Girod, Marion and MacAleese, Luke and Pieterse, Cornelius
                      Louwrens and Schlathoelter, Thomas and Techert, Simone and
                      Bari, Sadia},
      title        = {{T}he influence of the methionine residue on the
                      dissociation mechanisms of photoionized
                      methionine-enkephalin probed by {VUV} action spectroscopy},
      journal      = {The European physical journal / D},
      volume       = {75},
      number       = {4},
      issn         = {1434-6060},
      address      = {Heidelberg},
      publisher    = {Springer},
      reportid     = {PUBDB-2021-01567},
      pages        = {142},
      year         = {2021},
      abstract     = {VUV action spectroscopy has recently gained interest for
                      the study of peptides and proteins. However, numerous
                      aspects of the fundamental processes involved in the
                      photodissociation are yet to be understood. It can, for
                      example, be expected that sulfur-containing amino-acid
                      residues have a significant impact on the dissociation
                      processes following photoionization because of their
                      potential involvement in the transport of electron holes in
                      proteins. In order to investigate the influence of the
                      sulfur-containing methionine residue on the VUV
                      photodissociation of a small peptide a VUV action
                      spectroscopy study of gas-phase protonated
                      methionine-enkephalin and leucine-enkephalin in the photon
                      energy range of 6–35 eV was performed. The results show
                      that upon non-ionizing photoexcitation, the fragmentation
                      patterns of the two peptides are nearly identical, whereas
                      significant differences were observed upon photoionization.
                      The differences between the fragment yields and the
                      identified specific dissociation channels for
                      methionineenkephalin could be explained by the high electron
                      hole affinity of sulfur, which efficiently directs the
                      radical to the methionine side chain. Additionally, for both
                      peptides the presence of the intact photoionized precursor
                      ions was confirmed by their isotopic patterns and the
                      stability of these species could be evaluated.},
      cin          = {FS-SCS},
      ddc          = {530},
      cid          = {I:(DE-H253)FS-SCS-20131031},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / VH-NG-1104 - Structure and
                      dynamics of gas-phase biomolecules studied by photon-induced
                      ionization and dissociation $(2007_IVF-VH-NG-1104)$ / DFG
                      project 28586557 - SFB 755: Photonische Abbildungen auf der
                      Nanometerskala (28586557)},
      pid          = {G:(DE-HGF)POF4-633 / $G:(DE-HGF)2007_IVF-VH-NG-1104$ /
                      G:(GEPRIS)28586557},
      experiment   = {EXP:(DE-MLZ)External-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000733023100003},
      doi          = {10.1140/epjd/s10053-021-00147-y},
      url          = {https://bib-pubdb1.desy.de/record/456627},
}