Mass spectrometry has become the method of choice for the qualitative and quantitative
characterization of protein mixtures isolated from all kinds of living organisms. The raw data …

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 …

Glycosylation is perhaps the most common post-translational modification. Recently there
has been growing interest in cataloging the glycan structures, glycoproteins, and specific …

This Letter reviews efforts made to elucidate the mechanism by which electron-capture and
electron-transfer dissociation bond cleavages occur in mass spectrometry. The primary …

The lack of consensus sequence, common core structure, and universal endoglycosidase
for the release of O-linked oligosaccharides makes O-glycosylation more difficult to tackle …

We report the first detailed analysis at correlated levels of ab initio theory of experimentally
studied peptide cations undergoing charge reduction by collisional electron transfer and …

The effect of cation charge site on gas-phase ion/ion reactions between multiply protonated
model peptides and singly charged anions has been examined. Insights are drawn from the …

We have made use of classical dynamics trajectory simultions and ab initio electronic
structure calculations to estimate the cross sections with which electrons are attached (in …

The field of proteomics, the large-scale analysis of proteins, has undergone a huge
expansion over the past decade. Mass spectrometry-based proteomics relies on the …

Electron capture dissociation (ECD) and electron transfer dissociation (ETD) of doubly
protonated electron affinity (EA)-tuned peptides were studied to further illuminate the …