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 …

Abstract I. Introduction 162 II. CHARACTERISTICS OF TANDEM MASS SPECTRA OF
CARBOHYDRATES 163 A. Ionization of Carbohydrates 163 1. Electrospray Ionization (ESI) …

When non-mass spectrometrists are talking about mass spectrometry it rather often sounds
as if they were telling a story out of Poe's Tales of Mystery and Imagi-tion. Indeed, mass …

Neutralization-reionization mass spectrometry (MS) 1 is of unique value for preparing and
characterizing highly reactive and unstable neutral species, such as the intermediate in the …

For proteins of< 20 kDa, this new radical site dissociation method cleaves different and
many more backbone bonds than the conventional MS/MS methods (eg, collisionally …

Mass spectrometry has recently played a key role in the understanding of natural organic
matter (NOM) by providing molecular‐level details about its composition. NOM, a complex …

Characterization of larger proteins by mass spectrometry (MS) is especially promising
because the information complements that of classical techniques and can be obtained on …

Untitled Page 1 Page 2 JUNE 1, 2004 / ANALYTICAL CHEMISTRY 197 A he timeline for
maturation of a new measurement approach is difficult to predict but often accelerates as more …

Several approaches to ion activation in tandem mass spectrometry have been developed in
recent years for use in ion trapping instruments that allow for conditions to be reached …

Disulfide bonds in gaseous multiply-protonated proteins are preferentially cleaved in the
mass spectrometer by low-energy electrons, in sharp contrast to excitation of the ions by …