Mass spectrometry is a central technology in the life sciences, providing our most
comprehensive account of the molecular inventory of the cell. In parallel with developments …

Protein identification and peptide sequencing by tandem mass spectrometry requires
knowledge of how peptides fragment in the gas phase, specifically which bonds are broken …

Mass spectrometry (MS) has become a crucial technique for the analysis of protein
complexes. Native MS has traditionally examined protein subunit arrangements, while …

The most commonly used activation method in the tandem mass spectrometry (MS) of
peptides and proteins is energetic collisions with a neutral target gas. The overall process of …

This review presents a brief historical introduction to the development of tandem mass
spectrometry and its principal applications. It is placed in the context of the general …

Fragmentation at the Xxx-Pro bond was analyzed for a group of peptide mass spectra that
were acquired in a Finnigan ion trap mass spectrometer and were generated from proteins …

A kinetic model, based on the “mobile proton” model of peptide fragmentation, was
developed to quantitatively simulate the low-energy collision-induced dissociation (CID) …

A database of 5500 unique peptide tandem mass spectra acquired in an ion trap mass
spectrometer was assembled for peptides derived from proteins digested with trypsin …

The hydrolysis of crude egg white with pepsin, trypsin, and chymotrypsin produced peptides
with angiotensin-converting enzyme (ACE) inhibitory properties. These peptides were …

Data mining was performed on 28 330 unique peptide tandem mass spectra for which
sequences were assigned with high confidence. By dividing the spectra into different sets …