Ion mobility-mass spectrometry: a new paradigm for proteomics Conference Paper uri icon


  • Matrix-assisted laser desorption/ionization (MALDI) coupled with ion mobility-mass spectrometry (IM-MS) provides a rapid (s-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, -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. 2004 Elsevier B.V. All rights reserved.

published proceedings


altmetric score

  • 3

author list (cited authors)

  • McLean, J. A., Ruotolo, B. T., Gillig, K. J., & Russell, D. H.

citation count

  • 266

complete list of authors

  • McLean, JA||Ruotolo, BT||Gillig, KJ||Russell, DH

publication date

  • February 2005