Origin of product ions in the MS/MS spectra of peptides in a quadrupole ion trap
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Stored waveform inverse Fourier transform and double resonance techniques have been used in conjunction with a quadrupole ion trap to study the dissociation patterns of peptide ions. These experiments provide insight into the origin of individual product ions in an MS/MS spectrum. Results show for a series of leucine enkephalin analogues with five amino acid residues that the b 4 ion is the main product ion through which many other product ions arise. It was also observed that the percentage of the a 4 product ions that are formed directly from the protonated molecule (M+H)+ depends on the nature of the fourth amino acid residue. In addition, it was determined that in the peptides studied here lower series b ions (e.g., b 3 arise from direct dissociation of higher series b ions (e.g., b 4 only about 50% of the time.
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- 2.Barber, M.; Bordoli, R. S.; Sedgwick, R. D.; Tyler, A. N. J. Chem. Soc. Chem. Commun. 1981, 325.Google Scholar
- 4.Tandem Mass Spectrometry; McLafferty, F. W., Ed.; Wiley: New York, 1983.Google Scholar
- 5.Busch, K. L.; Glish, G. L.; McLuckey, S. A. Mass Spectrometry/Mass Spectrometry: Techniques and Applications in Tandem Mass Spectrometry; VCH: New York, 1988.Google Scholar
- 25.The resonance ejection frequency applied to resonantly eject the b 4 product ion of leucine enkephalin (YGGFL) was 84,805 Hz. Simulations using ITSIM  suggest that all b 4 product ions are resonantly ejected between 1 and 4 cycles of the applied resonant signal. This corresponds to a maximum time before ejection of about 50 µs.Google Scholar
- 28.Unpublished results.Google Scholar