Analysis of phosphorylated peptides by ion mobility-mass spectrometry. Academic Article uri icon

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.

published proceedings

  • Anal Chem

altmetric score

  • 3

author list (cited authors)

  • Ruotolo, B. T., Gillig, K. J., Woods, A. S., Egan, T. F., Ugarov, M. V., Schultz, J. A., & Russell, D. H.

citation count

  • 66

complete list of authors

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

publication date

  • November 2004