Journal
ANALYTICAL CHEMISTRY
Volume 82, Issue 2, Pages 579-584Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ac9018582
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Funding
- NIH National Center for Research Resources [P41 RR001614]
- Vincent J. Coates Foundation
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It is well established that protein sequence determination may be achieved by mass spectrometric analysis of protonated Untie peptide subjected to collisional activation. When separated by nanoflow HPLC, a high percentage of peptides from complex mixtures of proteins can usually be identified. Recently, alternative, radical-driven fragmentation approaches of electron capture dissociation and the more common electron transfer dissociation (ETD) have been introduced and made widely available. In order to utilize these techniques in large scale proteomics studies, it is important to characterize the performance of these fragmentation processes on peptides formed by a range of enzymatic cleavages. In this study, we present a statistical analysis of the ion types that are observed from peptides produced by different enzymes and highlight the different characteristics of ETD spectra of doubly charged precursors in comparison to precursors of higher charge states.
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