Berlin 2005 – wissenschaftliches Programm

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MS: Massenspektrometrie

MS 1: Ionenfallen

MS 1.1: Hauptvortrag

Freitag, 4. März 2005, 10:15–10:45, HU 3088

Electron Capture Dissociation in Fourier Transform Ion Cyclotron Resonance Mass Spectrometry — •Gökhan Baykut¹, Roland Jertz¹, Matthias Witt¹, Yury Tsybin², Roman Zubarev³, and Per Håkansson⁴ — ¹Bruker Daltonik GmbH, Bremen, Germany — ²National High Magnetic Field Laboratory, Tallahassee, FL — ³Biomedical Mass Spectrometry Center, University of Uppsala, Uppsala, Sweden — ⁴Division of Ion Physics, University of Uppsala, Uppsala, Sweden

Since its introduction in 1998, electron capture dissociation (ECD) has been successfully used in Fourier transform ion cyclotron resonance mass spectrometry of proteins and peptides. The capture of a low energy electron by a multiply protonated protein or polypeptide is an exoergic process which releases an energy in the range of 4−6 eV. This leads to a very fast fragmentation of the ion, estimated to be in a time range of 10⁻¹² s, which does not allow a redistribution of the reaction energy in the vibrational modes of the protonated protein (non-ergodic process). The fragmentation pattern resulting from ECD differs from a typical collision induced fragmentation (CID) or infrared multiphoton dissociation (IRMPD) process. For protein analysis and sequencing, this is complementary information. Additionally, the ECD process does not destroy some weaker bonds in post-translationally modified proteins and cleaves the peptide backbone. As the conventional ion fragmentation techniques like CID and IRMPD always cleave the weak bonds in the molecule, electron capture dissociation is considered as a promising new information source for biochemistry and biophysics of proteins.