Quantitative Proteomics Using Isobaric Chemical Tagging and HCD
Abstract:Multiplexed stable isotope reagents such as iTRAQ and Tandem Mass Tag (TMT) designed for MS/MS-based quantitation of peptides rely on accurate and robust detection of low mass fragments for peptide precursor ions. In the past, such analyses depended upon mass spectrometers capable of producing the so-called “triple-quadrupole-like” fragmentation including triple quadrupole mass spectrometers (TQMS) and quadrupole time-of-flight (Q-TOF) instruments. The “one-third rule” on an ion trap (IT) instrument precluded the use of these reagents on this widely available instrument platform until the invention of Pulsed Q Dissociation (PQD), which in itself manifests problems in generating sufficient reporter ion intensities for accurate quantitation. The introduction of high energy collisional-activated dissociation (HCD) on LTQ-Orbitrap XL and LTQ-Orbitrap Velos platforms has opened up great opportunities for accurate quantitative analysis of proteins and their post-translational modifications (PTMs) using chemical tagging by generating “triple- quadrupole-like” fragmentation mainly in the low mass range in MS/MS mode.
Document Type: Research Article
Publication date: 2011-04-01
More about this publication?
- Current Proteomics research in the emerging field of proteomics is growing at an extremely rapid rate. The principal aim of Current Proteomics is to publish well-timed review articles in this fast-expanding area on topics relevant and significant to the development of proteomics. Current Proteomics is an essential journal for everyone involved in proteomics and related fields in both academia and industry.