Robert Eisner and Iain H. McLean became friends after being introduced through their network colleague Joel Katz. Joining Robert to compile information, Iain was asked to write the full account in order to set the record straight once and for all following Robert's return from Barstow. Many months have been spent locating people, carrying out interviews, searching documents and investigating the facts about what actually happened in the desert between Los Angeles and Las Vegas in early 2008. The results of the research is a literal account of what happened to Robert Eisner during early 2008 in the Mojave Desert. "Barstow" is a relentless ride into the heart of the American psyche.

To advance the information content in biotechnology and nanotechnology studies using mass spectrometry (MS) techniques, two-dimensional (2D) post-ionization separations combining ion mobility (IM) with time-of-flight MS (IM-TOFMS) are described. The added data dimensionality consists of ion structural information based on the ion collision cross-section determined by IM with accurate mass measurements obtained by TOFMS. The basic theory of IM and practical implementation in IM-MS instrumentation is discussed and described in the context of high throughput separations (µs-ms), peptide and post-translational modification (PTM) identification, and structural determinations, for applications ranging from proteomics and tissue imaging, to characterization of carbon nanotubes.

Matrix-assisted laser desorption/ionization (MALDI) coupled with ion mobility–mass spectrometry (IM–MS) provides a rapid (μs–ms) means for the two-dimensional (2D) separation of complex biological samples (e.g., peptides, oligonucleotides, glycoconjugates, lipids, etc.), elucidation of solvent-free secondary structural elements (e.g., helices, β-hairpins, random coils, etc.), rapid identification of post-translational modifications (e.g., phosphorylation, glycosylation, etc.) or ligation of small molecules, and simultaneous and comprehensive sequencing information of biopolymers. In IM–MS, protein-identification information is complemented by structural characterization data, which is difficult to obtain using conventional proteomic techniques. New avenues for enhancing the figures of merit (e.g., sensitivity, limits of detection, dynamic range, and analyte selectivity) and optimizing IM–MS experimental parameters are described in the context of deriving new information at the forefront of proteomics research. Keywords: Ion mobility; Mass spectrometry; Ion mobility-mass spectrometry; Proteomics; Biopolymers

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Molecular profiling and imaging mass spectrometry (IMS) of tissues can often result in complex spectra that are difficult to interpret without additional information about specific signals. This report describes increasing data dimensionality in IMS by combining two-dimensional separations at each spatial location on the basis of imaging ion mobility-mass spectrometry (IM-MS). Analyte ions are separated on the basis of both ion-neutral collision cross section and m/z, which provides rapid separation of isobaric, but structurally distinct ions. The advantages of imaging using ion mobility prior to MS analysis are demonstrated for profiling of human glioma and selective lipid imaging from rat brain. Copyright © 2007 John Wiley & Sons, Ltd.

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