Journal
JOURNAL OF MASS SPECTROMETRY
Volume 39, Issue 4, Pages 361-367Publisher
WILEY
DOI: 10.1002/jms.592
Keywords
proteomics; matrix-assisted laser desorption/ionization; separation; peptides; conformation
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Ion mobility mass spectrometry (IM-MS) peptide mass mapping experiments were performed using a variety of drift gases (He, N-2, Ar and CH4). The drift gases studied cover a range of polarizabilities ((0.2-2.6) x 10(-24) cm(3)) and the peak capacities obtained for tryptic peptides in each gas are compared. Although the different gases exhibit similar peak capacities (5430 (Ar) to 7580 (N-2)) in some cases separation selectivity presumably based on peptide conformers (or conformer populations), is observed. For example the drift time profiles observed for some tryptic peptide ions from aldolase (rabbit muscle) show a dependence on drift gas. The transmission of high-mass ions (m/z > 2000) is also influenced by increased scattering cross-section of the more massive drift gases. Consequently the practical peak capacity for IM-MS separation cannot be assumed to be solely a function of resolution and the ability of a gas to distribute signals in two-dimensional space; rather, peak capacity estimates must account for the transmission losses experienced for peptide ions as the drift gas mass increases. Copyright (C) 2004 John Wiley Sons, Ltd.
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