(MS) and MS-driven proteomics have continued to develop as the premier tools for
characterizing proteome composition, structure, and function. 2 The new era of proteomics …

For about three decades, the chemistry of cation radicals derived from organic molecules
had received a major impetus from mass spectrometry. This was because cation radicals …

Electron-transfer dissociation (ETD) delivers the unique attributes of electron capture
dissociation to mass spectrometers that utilize radio frequency trap**-type devices (eg …

Progress in structural biology research has led to a high demand for powerful and yet
complementary analytical tools for structural characterization of proteins and protein …

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 …

Hydrogen (1H/2H) exchange combined with mass spectrometry (HX− MS) has become a
recognized method for the analysis of protein structural dynamics. Presently, the …

Mass spectrometry is routinely applied to measure the incorporation of deuterium into
proteins and peptides. The exchange of labile, heteroatom-bound hydrogens is mainly used …

Here we report the first implementation of activated ion electron transfer dissociation (AI-
ETD) for top down protein characterization, showing that AI-ETD definitively extends the m/z …

Hydrogen rearrangement is an important process in radical chemistry. A high degree of H·
rearrangement to and from z· ionic fragments (combined occurrence frequency 47 …

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