Peptide and Protein Characterization by High Rate Electron Capture Dissociation Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
2004 (English)In: Journal of Mass Spectrometry, ISSN 1076-5174, Vol. 39, no 7, 719-729 p.Article in journal (Refereed) Published
The analytical utility of the electron capture dissociation (ECD) technique, developed by McLafferty and co-workers, has substantially improved peptide and protein characterization using Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS). The limitations of the first ECD implementations on commercial instruments were eliminated by the employment of low-energy electron-injection systems based on indirectly heated dispenser cathodes. In particular, the ECD rate and reliability were greatly increased, enabling the combination of ECD/FTICR-MS with on-line liquid separation techniques. Further technique development allowed the combination of two rapid fragmentation techniques, high-rate ECD and infrared multiphoton dissociation (IRMPD), in a single experimental configuration. Simultaneous and consecutive irradiations of trapped ions with electrons and photons extended the possibilities for ion activation/dissociation and led to improved peptide and protein characterization. The application of high-rate ECD/FTICR-MS has demonstrated its power and unique capabilities in top-down sequencing of peptides and proteins, including characterization of post-translational modifications, improved sequencing of peptides with multiple disulfide bridges and secondary fragmentation (w-ion formation). Analysis of peptide mixtures has been accomplished using high-rate ECD in bottom-up mass spectrometry based on mixture separation by liquid chromatography and capillary electrophoresis. This paper summarizes the current impact of high-rate ECD/FTICR-MS for top-down and bottom-up mass spectrometry of peptides and proteins.
Place, publisher, year, edition, pages
2004. Vol. 39, no 7, 719-729 p.
Posttranslational modification, Mass spectrometry, Ion cyclotron resonance spectrometry, Fourier transformation, Electron capture, Protein, Peptides
IdentifiersURN: urn:nbn:se:uu:diva-91521DOI: 10.1002/chin.200523298OAI: oai:DiVA.org:uu-91521DiVA: diva2:164284