Analysis of phosphorylated peptides by ion mobility-mass spectrometry

Brandon T. Ruotolo, Kent J. Gillig, Amina S. Woods, Thomas F. Egan, Michael V. Ugarov, J. Albert Schultz, David H. Russell

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An ion mobility-mass spectrometry technique for rapid screening of phosphopeptides in protein digests is described. A data set of 43 sequences (ranging in mass from 400 to 3000 m/z) of model and tryptic peptides, including serine, threonine, and tyrosine phosphorylation, was investigated, and the data support our previously reported observation (Ruotolo, B. T.; Verbeck, G. F., IV; Thomson, L. M.; Woods, A. S.; Gillig, K. J.; Russell, D. H. J. Proteome Res. 2002, 1, 303.) that the drift time-m/z relationship for singly charged phosphorylated peptide ions is different from that for nonphosphorylated peptides. The data further illustrate that a combined data-dependent IM-MS/MS approach for phosphopeptide screening would have enhanced throughput over conventional MS/MS-based methodologies.

Original languageEnglish (US)
Pages (from-to)6727-6733
Number of pages7
JournalAnalytical Chemistry
Issue number22
StatePublished - Nov 15 2004
Externally publishedYes

ASJC Scopus subject areas

  • Analytical Chemistry


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