CID,ETD and HCD Fragmentation to Study Protein Post-Translational Modifications

Abstract

Copyright: © 2013 Quan L. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Gas phase biomolecule-ion chemistry has played a crucial role in mass spectrometry (MS) based proteomics study. The key step generating the structure information of a protein or a peptide is by ion dissociation or transformation to the characteristic tandem mass spectrometry spectra (MS2) fragmentation patterns. Collision-induced dissociation (CID) is the most widely applied fragmentation method for proteome identification and quantification analysis. Under CID condition, the peptide/protein precursor ion undergoes one or more collisions by interactions with neutral gas molecules, contributing to vibrational energy which will redistribute over the peptide/protein ion. The vibrational energy can result in ion dissociation occurring at amide bonds along the peptide backbone, generating band y-type fragment ions or leading to losses of small neutral molecules, such as water and/ or ammonia or other fragments derived from side chains [1].