Ruotolo Brandon T, Gillig Kent J, Woods Amina S, Egan Thomas F, Ugarov Michael V, Schultz J Albert, Russell David H
Laboratory for Biological Mass Spectrometry, Department of Chemistry, Texas A&M University, College Station, Texas 77843, USA.
Anal Chem. 2004 Nov 15;76(22):6727-33. doi: 10.1021/ac0498009.
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.
本文描述了一种用于快速筛选蛋白质消化物中磷酸肽的离子淌度-质谱技术。研究了一组包含丝氨酸、苏氨酸和酪氨酸磷酸化的43个模型肽和胰蛋白酶肽序列（质量范围为400至3000 m/z）的数据集，数据支持了我们之前报道的观察结果（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.），即单电荷磷酸化肽离子的淌度时间-m/z关系与非磷酸化肽不同。数据进一步表明，用于磷酸肽筛选的组合数据依赖型离子淌度-串联质谱方法比传统的基于串联质谱的方法具有更高的通量。
