Journal of the American Society for Mass Spectrometry

, Volume 20, Issue 10, pp 1775–1781

The mass-mobility correlation redux: The conformational landscape of anhydrous biomolecules

Critical Insight

DOI: 10.1016/j.jasms.2009.06.016

Cite this article as:
McLean, J.A. J Am Soc Mass Spectrom (2009) 20: 1775. doi:10.1016/j.jasms.2009.06.016

Abstract

Structural separations on the basis of gas-phase ion mobility-mass spectrometry are increasingly used for the analysis of complex biological samples. As a tool to elucidate biomolecular structure, ion mobility-mass spectrometry methods are unique in that direct molecular structural information is obtained for all resolved species, largely irrespective of the complexity of the sample. Computational approaches are used to interpret and discern structural details consistent with the empirical results. To a first approximation, correlations of mobility with mass allow for qualitative identification of the molecular class to which a particular species belongs. These correlations allow simultaneous characterization of different classes of biomolecules, which provides a means for combining omics measurements, such as lipidomics, proteomics, glycomics, and metabolomics, in the same analysis. Examination of the correlation of fine structure reveals that specific structural motifs, chemical functionality, chemical connectivity, and composition may also be determined, depending on the specific biomolecular class. Mapping the coarse and fine structure in ion mobility-mass spectrometry conformation space measurements provides an atlas for interpretation and discovery in complicated spectra.

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© American Society for Mass Spectrometry 2009

Authors and Affiliations

  1. 1.Department of Chemistry, Vanderbilt Institute of Chemical Biology, Vanderbilt Institute for Integrative Biosystems Research and EducationVanderbilt UniversityNashvilleUSA