In recent years, electron capture (ECD) and electron transfer dissociation (ETD) have
emerged as two of the most useful methods in mass spectrometry‐based protein analysis …

Electron capture dissociation (ECD) is a tandem mass spectrometry (MS/MS) method that
utilizes the interaction of ions and electrons. Its unique ability to preserve labile bonds …

This tutorial review describes the principles and practices of electron capture and transfer
dissociation (ECD/ETD or ExD) mass spectrometry (MS) employed for peptide and protein …

Peptide and protein characterization by mass spectrometry (MS) relies on their dissociation
in the gas phase into specific fragments whose mass values can be aligned as 'mass …

Top-down proteomics by mass spectrometry (MS) involves the mass measurement of an
intact protein followed by subsequent activation of the protein to generate product ions …

Proteomics analysis using tandem mass spectrometry requires informative backbone
fragmentation of peptide ions. Collision-activated dissociation (CAD) of cations alone is not …

It is well established that protein sequence determination may be achieved by mass
spectrometric analysis of protonated tryptic peptides subjected to collisional activation …

Tandem mass spectrometry (MS/MS) provides detailed information for structural
characterization of biomolecules. The combination of electron capture dissociation (ECD) …

New ion fragmentation technologies—electron capture dissociation (ECD) and electron-
transfer dissociation (ETD)—are based on interaction of multiply charged polypeptides with …

Electron-based fragmentation methods have revolutionized biomolecular mass
spectrometry, in particular native and top-down protein analysis. Here, we report the use of a …