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 …

Disulfide bonds are important structural moieties of proteins: they ensure proper folding,
provide stability, and ensure proper function. With the increasing use of proteins for …

Thermolysin hydrolyzates of freshly isolated, extensively stored (6 years, 6° C, dry) and
heated (60 min, 90° C, in excess water) bovine serum albumin (BSA) samples were …

Introduction: Mass spectrometry (MS) is widely used in the characterization of biomolecules
including peptide and protein therapeutics. These biotechnology products have seen rapid …

Monoclonal antibodies (mAbs) are important therapeutic glycoproteins, but their large size
and structural complexity make them difficult to rapidly characterize. Top-down mass …

Disulfide bonds in proteins have a substantial impact on protein structure, stability, and
biological activity. Localizing disulfide bonds is critical for understanding protein folding and …

Pairing light and heavy chains in monoclonal antibodies (mAbs) using top-down (TD) or
middle-down (MD) mass spectrometry (MS) may complement the sequence information on …

Alongside the success of protein-based bio-therapeutics over the last decades and
facilitated by advances both in protein engineering and manufacturing, new product formats …

We report on the dissociation of singly protonated peptides by electrons using electron-
activated dissociation (EAD), which comprises electron impact excitation of ions from …

A novel electrochemical (EC) method for fast and efficient reduction of the disulfide bonds in
proteins and peptides is presented. The method does not use any chemical agents and is …