Mass Spectrometry

This article describes the ability to increase the sensitivity for a target compound in the presence of high-level background impurities by removing the dosing vehicle using a high-field asymmetric waveform ion mobility spectrometry gas-phase separation before mass spectrometry analysis.

Liquid chromatography with tandem mass spectrometry (LC–MS-MS) led to a revolution in environmental testing. The coupling of liquid chromatography with tandem mass spectrometry created a powerful analytical tool for the analysis of emerging environmental contaminants. Pharmaceuticals and personal care products, perfluorinated compounds, brominated flame retardants, and disinfection byproducts were chosen as examples to illustrate the use of this new technique in environmental analysis.

Successful characterization of protein posttranslational modifications (PTMs) is critical to our understanding of many biological processes. Unfortunately, attempts to describe PTMs often prove experimentally difficult and result in ambiguous conclusions. As technologies in the field of mass spectrometry (MS) continue to improve, people are turning increasingly to mass spectral techniques for PTM characterization. Recently, novel modes of peptide fragmentation have emerged that are giving scientists greater ability to elucidate protein posttranslational modification. One example is electron-capture dissociation (ECD), an alternative fragmentation mechanism for use in peptide analysis via tandem mass spectrometry. ECD selectively cleaves N-Cα bonds of the peptide backbone, yielding c- and z-ions without the loss of labile PTMs. ECD therefore holds advantages over conventional fragmentation techniques such as collisionally induced dissociation (CID), which often cleave PTMs from the peptide backbone,..

The matter of perfluorinated compounds (PFCs) came to focus at the United States Environmental Protection Agency (EPA) some eight years ago.

Recent work suggests that the practical value of hyphenated techniques is limited by difficulties inherent in achieving definitive compositional answers in general MS. This article argues that it is not impossible in certain cases.

Nearly a dozen incipient technologies have appeared in recent years. Which will survive? Which will find extensive, robust usage as did electrospray ionization? Which are fated to become footnotes in mass spectrometry practice?

"As research advances, about half of what we will teach you . . . will turn out to be wrong. The problem is, we presently don't know which half." Powerful Medicines, Jerry Avorn, 2004

Understanding how imaging can advance life science research and what issues need to be addressed to unlock the true potential of mass spectrometry-based imaging raises awareness of new possibilities for researchers. This article explores mass spectrometry imaging, aiming to educate about scientific opportunities to consider and the pitfalls to avoid.

This month's installment of "MS - The Practical Art" provides a slightly different view of how practitioners employ the skills of interpretation that have been the focus in recent columns.

This month's column brings much of the previous discussion on how to interpret mass spectra to a practical examination of detecting substitutions in counterfeit pharmaceuticals.

In this month's "MS-The Practical Art," Michael Balogh takes a closer look at insight provided by Chuck McEwen regarding obstacles while using solvents.

Serum protein profiling using mass spectrometry (MS) is one of the most promising approaches for biomarker identification.

In Part I of this two-part look at spectral interpretation, Michael Balogh examined the ability to see and appreciate the product of our analytical devices. In Part II, he takes a closer look at the tools of the trade.

Despite their different levels of technological maturity, CE and LC coupled with electrospray ionization MS techniques can be operated at the same level of automation. However, they differ in their configuration, selectivity, sensitivity, and method development.

Current sample preparation procedures for LC–MS as applied to samples from biological matrices.