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Grazing incidence surface-induced dissociation of protonated peptides generated by matrix-assisted laser desorption/ionization

✍ Scribed by Andreas Wieghaus; Lothar Schmidt; Anna M. Popova; Viatcheslav V. Komarov; Hartmut Jungclȧs


Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
135 KB
Volume
14
Category
Article
ISSN
0951-4198

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✦ Synopsis


The grazing incidence surface-induced dissociation (GI-SID) of various protonated peptides with typical kinetic energies of 350 eV was investigated. Peptide ions were generated by matrix-assisted laser desorption/ ionization (MALDI) using delayed extraction. The collision target surfaces used were aluminum and a liquid film of perfluorinated hydrocarbons. All peptides studied in these experiments showed enhanced fragment ion yields at grazing incidence (GI-SID effect) as observed in our former experiments with other precursor ion types. In general the GI-SID spectra exhibit N-terminal a 1 -type fragment ions, immonium ions and side-chain fragment ions in the low mass-to-charge region. Fragment ion series of the peptide backbone were not observed, which are typical and abundant in the spectra of established fragmentation techniques like collision-induced dissociation, MALDI post-source decay or surface-induced dissociation at steeper angles. The potential of the GI-SID process to yield useful information for primary structure determination of peptides is indicated by the observed differences in the GI-SID spectra of the isomeric dipeptides LR and IR.


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