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Boundaries of Mass Resolution in Native Mass Spectrometry

  • Critical Insight
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Journal of The American Society for Mass Spectrometry

Abstract

Over the last two decades, native mass spectrometry (MS) has emerged as a valuable tool to study intact proteins and noncovalent protein complexes. Studied experimental systems range from small-molecule (drug)–protein interactions, to nanomachineries such as the proteasome and ribosome, to even virus assembly. In native MS, ions attain high m/z values, requiring special mass analyzers for their detection. Depending on the particular mass analyzer used, instrumental mass resolution does often decrease at higher m/z but can still be above a couple of thousand at m/z 5000. However, the mass resolving power obtained on charge states of protein complexes in this m/z region is experimentally found to remain well below the inherent instrument resolution of the mass analyzers employed. Here, we inquire into reasons for this discrepancy and ask how native MS would benefit from higher instrumental mass resolution. To answer this question, we discuss advantages and shortcomings of mass analyzers used to study intact biomolecules and biomolecular complexes in their native state, and we review which other factors determine mass resolving power in native MS analyses. Recent examples from the literature are given to illustrate the current status and limitations.

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Acknowledgments

This work, and in particular PL and AJRH, has been supported by the ManiFold project, grant agreement number 317371, and in part by the PRIME-XS project, grant agreement number 262067, both funded by the European Union 7th Framework Programme. The Netherlands Proteomics Centre, embedded in The Netherlands Genomics Initiative, is acknowledged for funding.

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  1. Biomolecular Mass Spectrometry and Proteomics, Bijvoet Centre for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands

    Philip Lössl, Joost Snijder & Albert J. R. Heck

  2. Netherlands Proteomics Center, Padualaan 8, 3584 CH, Utrecht, The Netherlands

    Philip Lössl, Joost Snijder & Albert J. R. Heck

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  1. Philip Lössl
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Lössl, P., Snijder, J. & Heck, A.J.R. Boundaries of Mass Resolution in Native Mass Spectrometry. J. Am. Soc. Mass Spectrom. 25, 906–917 (2014). https://doi.org/10.1007/s13361-014-0874-3

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