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Selective detection and identification of phosphopeptides by dansyl MS/MS/MS fragmentation
Author(s) -
Amoresano Angela,
Monti Gianluca,
Cirulli Claudia,
Marino Gennaro
Publication year - 2006
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.2461
Subject(s) - chemistry , tandem mass spectrometry , mass spectrometry , fragmentation (computing) , proteomics , chromatography , phosphorylation , ion trap , protein phosphorylation , computational biology , biochemistry , gene , biology , computer science , operating system , protein kinase a
Abstract Protein phosphorylation regulates many cellular processes and pathways, such as cell cycle progression, signal transduction cascades and gene expression. Selective detection of phosphopeptides from proteolytic digests is a challenging and highly relevant task in many proteomics applications. Often phosphopeptides are present in small amounts and need selective isolation or enrichment before identification. Here we report a novel approach to label selectively phospho‐Ser/‐Thr residues by exploiting the features of a novel linear ion trap mass spectrometer. Using dansyl labelling and MS 3 fragmentation, we developed a method useful for the large‐scale proteomic profiling of phosphorylation sites. The new residues in the sequence were stable and easily identifiable under general conditions for tandem mass spectrometric sequencing. Copyright © 2006 John Wiley & Sons, Ltd.