Analysis of phosphorylated peptides by ion mobility-mass spectrometry.
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.
Ruotolo
Brandon T
BT
Laboratory for Biological Mass Spectrometry, Department of Chemistry, Texas A&M University, College Station, Texas 77843, USA.
Gillig
Kent J
KJ
Woods
Amina S
AS
Egan
Thomas F
TF
Ugarov
Michael V
MV
Schultz
J Albert
JA
Russell
David H
DH
D000595:Amino Acid Sequence; D007477:Ions; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010455:Peptides / Q000737:chemistry*; D010766:Phosphorylation; D014357:Trypsin / Q000737:chemistry
D007477:Ions; D010455:Peptides; D014357:Trypsin