Fragmentation of amidinated peptide ions

The collision-induced dissociation characteristics of amidinated and unmodified tryptic peptides are compared using an ion trap mass spectrometer with both electrospray ionization and matrix-assisted laser/desorption ionization (MALDI). Several fragmentation pathways in a number of tryptic peptides...

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Veröffentlicht in:	Journal of the American Society for Mass Spectrometry 2004-02, Vol.15 (2), p.158-167
Hauptverfasser:	Beardsley, Richard L, Reilly, James P
Format:	Artikel
Sprache:	eng
Schlagworte:	Amides - chemistry Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Biological and medical sciences Chemistry Desorption Exact sciences and technology Fragmentation Fundamental and applied biological sciences. Psychology Ionization Ions Ions - chemistry Mass spectrometry Molecular Sequence Data Molecular Structure Organic chemistry Peptide Fragments - chemistry Peptides Peptides - chemistry Proteins Reactivity and mechanisms Spectrometry, Mass, Electrospray Ionization Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Beschreibung
Zusammenfassung:	The collision-induced dissociation characteristics of amidinated and unmodified tryptic peptides are compared using an ion trap mass spectrometer with both electrospray ionization and matrix-assisted laser/desorption ionization (MALDI). Several fragmentation pathways in a number of tryptic peptides of various precursor charge states are found to be enhanced. The additional information conveyed by the observed fragment ions should facilitate protein identifications.
ISSN:	1044-0305 1879-1123
DOI:	10.1016/j.jasms.2003.10.007