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

doi:10.1021/ac0498009

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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65 Scopus citations

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.

Original language	English (US)
Pages (from-to)	6727-6733
Number of pages	7
Journal	Analytical Chemistry
Volume	76
Issue number	22
DOIs	https://doi.org/10.1021/ac0498009
State	Published - Nov 15 2004
Externally published	Yes

ASJC Scopus subject areas

Analytical Chemistry

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10.1021/ac0498009

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title = "Analysis of phosphorylated peptides by ion mobility-mass spectrometry",

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.",

author = "Ruotolo, {Brandon T.} and Gillig, {Kent J.} and Woods, {Amina S.} and Egan, {Thomas F.} and Ugarov, {Michael V.} and Schultz, {J. Albert} and Russell, {David H.}",

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T1 - Analysis of phosphorylated peptides by ion mobility-mass spectrometry

AU - Ruotolo, Brandon T.

AU - Gillig, Kent J.

AU - Woods, Amina S.

AU - Egan, Thomas F.

AU - Ugarov, Michael V.

AU - Schultz, J. Albert

AU - Russell, David H.

PY - 2004/11/15

Y1 - 2004/11/15

N2 - 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.

AB - 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.

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Analysis of phosphorylated peptides by ion mobility-mass spectrometry

Abstract

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