Analysis of Phosphorylated Peptides by Ion Mobility-Mass Spectrometry

Citations Over TimeTop 14% of 2004 papers

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.

Related Papers

• → Amino acid distributions around O-linked glycosylation sites(1991)279 cited
• → Analysis of Protein Phosphorylation in the Regions of Consecutive Serine/Threonine Residues by Negative Ion Electrospray Collision-Induced Dissociation. Approach to Pinpointing of Phosphorylation Sites(2007)28 cited
• → A study on L-threonine and L-serine uptake in Escherichia coli K-12(2023)5 cited
• → THE DESTRUCTION OF SERINE AND THREONINE DURING ACID HYDROLYSIS(1969)32 cited
• → Synthesis of phosphopeptides: A simple phosphorylation procedure for serine and threonine(1987)21 cited