
pmid: 14766283
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.
Ions, Spectrometry, Mass, Electrospray Ionization, Molecular Structure, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Molecular Sequence Data, Amino Acid Sequence, Peptides, Amides, Peptide Fragments
Ions, Spectrometry, Mass, Electrospray Ionization, Molecular Structure, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Molecular Sequence Data, Amino Acid Sequence, Peptides, Amides, Peptide Fragments
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