| Literature DB >> 15538797 |
Brandon T Ruotolo1, Kent J Gillig, Amina S Woods, Thomas F Egan, Michael V Ugarov, J Albert Schultz, David H Russell.
Abstract
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.Entities:
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Year: 2004 PMID： 15538797 DOI： 10.1021/ac0498009
Source DB: PubMed Journal: Anal Chem ISSN： 0003-2700 Impact factor: 6.986