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Native mass spectrometry: a bridge between interactomics and structural biology

Nature Methods volume 5, pages 927–933 (2008)Cite this article

Abstract

Native mass spectrometry is an emerging technology that allows the topological investigation of intact protein complexes with high sensitivity and a theoretically unrestricted mass range. This unique tool provides complementary information to established technologies in structural biology, and also provides a link to high-throughput interactomics studies, which do not generate information on exact protein complex-composition, structure or dynamics. Here I review the current state of native mass spectrometry technology and discuss several important biological applications. I also describe current experimental challenges in native mass spectrometry, encouraging readers to contribute to solutions.

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Figure 1: Denatured and native mass spectra of H. pylori urease.
Figure 2: Tandem mass spectrometry of the intact 517 kDa RNA Pol II complex.
Figure 3: The ins and outs of native mass spectrometry.
Figure 4: Native mass spectra of intact HBV viral capsids.

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Acknowledgements

I thank all colleagues in native MS who have contributed in making this area of research come to maturity. I acknowledge all members of my group, most notably the native MS (former) members whose material and input I have used here; K. Lorenzen, H. Mazon, M. Pinkse, S. Synowsky, C. Uetrecht, R. van den Heuvel, E. van Duijn and C. Versluis. K. Lorenzen and C. Uetrecht helped construct the figures. Additionally, I thank all collaborators whose samples, support and expertise have been instrumental in our work.

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  1. Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, Utrecht, 3584, CA, The Netherlands

    Albert J R Heck

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Correspondence to Albert J R Heck.

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Heck, A. Native mass spectrometry: a bridge between interactomics and structural biology. Nat Methods 5, 927–933 (2008). https://doi.org/10.1038/nmeth.1265

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