Electron Capture Dissociation Mass Spectrometry in Characterization of Peptides and Proteins
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Electron capture dissociation (ECD) represents one of the most recent and significant advancements in tandem mass spectrometry (MS/MS) for the identification and characterization of polypeptides. In comparison with the conventional fragmentation techniques, such as collisionally activated dissociation (CAD), ECD provides more extensive sequence fragments, while allowing the labile modifications to remain intact during backbone fragmentation—an important attribute for characterizing post-translational modifications. Herein, we present a brief overview of the ECD technique as well as selected applications in characterization of peptides and proteins. Case studies including characterization and localization of amino acid glycosylation, methionine oxidation, acylation, and “top–down” protein mass spectrometry using ECD will be presented. A recent technique, coined as electron transfer dissociation (ETD), will be also discussed briefly.
Key wordsElectron capture dissociation Electron transfer dissociation Electrospray ionization Fourier transform mass spectrometry Post-translational modifications
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We wish to thank Professor F.W. McLafferty and Dr. Y. Ge for kindly providing Figures 2 and 6.
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