NDLI: Pseudo-MS$^{3}$ in a MALDI orthogonal quadrupole-time of flight mass spectrometer

Content Provider	Springer Nature Link
Author	Raska, Christina S. Parker, Carol E. Huang, Cai Han, Jun Glish, Gary L. Pope, Marshall Borchers, Christoph H.
Copyright Year	2002
Abstract	Both the matrix selected and the laser fluence play important roles in MALDI-quadrupole/time of flight (QqTOF) fragmentation processes. “Hot” matrices, such as α-cyano-4-hydroxy-cinnamic acid (HCCA), can increase fragmentation in MS spectra. Higher laser fluence also increases fragmentation. Typical peptide fragment ions observed in the QqTOF are a, b, and y ion series, which resemble low-energy CID product ions. This fragmentation may occur in the high-pressure region before the first mass-analyzing quadrupole. Fragment ions can be selected by the first quadrupole (Q1), and further sequenced by conventional MS/MS. This allows pseudo-MS$^{3}$ experiments to be performed.For peptides of higher molecular weight, pseudo-MS$^{3}$ can extend the mass range beyond what is usually accessible for sequencing, by allowing one to sequence a fragment ion of lower molecular weight instead of the full-length peptide. Peptides that predominantly show a single product ion after MS/MS yield improved sequence information when this technique is applied. This method was applied to the analysis of an in vitro phosphorylated peptide, where the intact enzymatically-generated peptide showed poor dissociation via MS/MS. Sequencing a fragment ion from the phosphopeptide enabled the phosphorylation site to be unambiguously determined.
Starting Page	1034
Ending Page	1041
Page Count	8
File Format	PDF
ISSN	10440305
Journal	Journal of The American Society for Mass Spectrometry
Volume Number	13
Issue Number	9
e-ISSN	18791123
Language	English
Publisher	Springer-Verlag
Publisher Date	2002-01-01
Publisher Institution	The American Society for Mass Spectrometry
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Analytical Chemistry Biotechnology Organic Chemistry Proteomics Bioinformatics
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Structural Biology

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