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Issue 5, 2010
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Ion mobility mass spectrometry of proteins and proteinassemblies

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Traditionally, mass spectrometry has been a powerful analytical method enabling the structural analysis of small molecules, and later on peptides and proteins. With the advent of native mass spectrometry, using a combination of electrospray ionisation and time of flight analysis, mass spectrometry could also be applied to the mass determination of large protein complexes such as ribosomes and whole viruses. More recently, ion mobility has been coupled to mass spectrometry providing a new dimension in the analysis of biomolecules, with ion mobility separating ions according to differences in size and shape. In the context of native mass spectrometry, ion mobility mass spectrometry opens up avenues for the detailed structural analysis of large and heterogeneous protein complexes, providing information on the stoichiometry, topology and cross section of these assemblies and their composite subunits. With these characteristics, ion mobility mass spectrometry offers a complementary tool in the context of structural biology. Here, we critically review the development, instrumentation, approaches and applications of ion mobility in combination with mass spectrometry, focusing on the analysis of larger proteins and proteinassemblies (185 references).

Graphical abstract: Ion mobility mass spectrometry of proteins and protein assemblies

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Article information

13 Jul 2009
First published
25 Nov 2009

Chem. Soc. Rev., 2010,39, 1633-1655
Article type
Critical Review

Ion mobility mass spectrometry of proteins and proteinassemblies

C. Uetrecht, R. J. Rose, E. van Duijn, K. Lorenzen and A. J. R. Heck, Chem. Soc. Rev., 2010, 39, 1633
DOI: 10.1039/B914002F

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