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Native Mass Spectrometry: Towards High-Throughput Structural Proteomics

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Structural Proteomics

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1261))

Abstract

Native mass spectrometry (MS) has become a sensitive method for structural proteomics, allowing practitioners to gain insight into protein self-assembly, including stoichiometry and three-dimensional architecture, as well as complementary thermodynamic and kinetic aspects. Although MS is typically performed in vacuum, a body of literature has described how native solution-state structure is largely retained on the timescale of the experiment. Native MS offers the benefit that it requires substantially smaller quantities of a sample than traditional structural techniques such as NMR and X-ray crystallography, and is therefore well suited to high-throughput studies. Here we first describe the native MS approach and outline the structural proteomic data that it can deliver. We then provide practical details of experiments to examine the structural and dynamic properties of protein assemblies, highlighting potential pitfalls as well as principles of best practice.

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    Authors and Affiliations

    1. Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK

      Frances D. L. Kondrat, Weston B. Struwe & Justin L. P. Benesch

    2. Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK

      Frances D. L. Kondrat, Weston B. Struwe & Justin L. P. Benesch

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    1. Frances D. L. Kondrat
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    2. Weston B. Struwe
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    3. Justin L. P. Benesch
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    Correspondence to Justin L. P. Benesch .

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    Editors and Affiliations

    1. Oxford Protein Production Facility UK, Didcot, Oxfordshire, United Kingdom

      Raymond J. Owens

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    Kondrat, F.D.L., Struwe, W.B., Benesch, J.L.P. (2015). Native Mass Spectrometry: Towards High-Throughput Structural Proteomics. In: Owens, R. (eds) Structural Proteomics. Methods in Molecular Biology, vol 1261. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2230-7_18

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    • DOI: https://doi.org/10.1007/978-1-4939-2230-7_18

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