A Century of Progress in Molecular Mass Spectrometry

Abstract

The first mass spectrum of a molecule was measured by J.J. Thomson in 1910. Mass spectrometry (MS) soon became crucial to the study of isotopes and atomic weights and to the development of atomic weapons for World War II. Its notable applications to molecules began with the quantitative analysis of light hydrocarbons during World War II. When I joined the Dow Chemical Company in 1950, MS was not favored by organic chemists. This situation improved only with an increased understanding of gaseous ion chemistry, which was obtained through the use of extensive reference data. Gas chromatography–MS was developed in 1956, and tandem MS was first used a decade later. In neutralization-reionization MS, an unusual, unstable species is prepared by ion-beam neutralization and characterized by reionization. Electrospray ionization of a protein mixture produces its corresponding ionized molecules. In top-down proteomics, ions from an individual component can be mass separated and subjected to collision-activated and electron-capture dissociation to provide extensive sequence information.

Progress in Top-Down Proteomics and the Analysis of Proteoforms

“…Fred McLafferty (12) penned a fascinating exploration of the history of molecular MS and the dawning of proteomics for this journal in 2011. In the Future Issues section of that review, the first item predicted that TDP would become a routine technique for the characterization of larger proteins in complex mixtures (12).…”

“…In the Future Issues section of that review, the first item predicted that TDP would become a routine technique for the characterization of larger proteins in complex mixtures (12). Just five years later, the field of top-down has rapidly advanced to begin the realization of this vision, thanks to improvements in MS tools and processes that are detailed here.…”

Order of Magnitude Signal Gain in Magnetic Sector Mass Spectrometry Via Aperture Coding

“…M ass spectrometers are versatile analytical laboratory instruments because they are fast, accurate, sensitive, selective, and can accommodate a wide variety of sample types [1][2][3][4]. However, in situ measurements with mass spectrometers in field settings are difficult because of the size, cost, and complexity of the instrument.…”

Database independent proteomics analysis of the ostrich and human proteome

“…Proteomic analysis by MS has taken on this challenge, utilizing the increasing sensitivity and peptide sequencing speed of MS instruments and getting closer to mapping complete proteomes (1,2). Sequencing proteolytic peptides using fragmentation by collision-induced dissociation (CID) is common practice in high throughput proteome analyses.…”