Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2020 Oct;55(10):e4578.
doi: 10.1002/jms.4578.

Native mass spectrometry-A valuable tool in structural biology

Affiliations

Native mass spectrometry-A valuable tool in structural biology

Marie Barth et al. J Mass Spectrom. 2020 Oct.

Abstract

Proteins and the complexes they form with their ligands are the players of cellular action. Their function is directly linked with their structure making the structural analysis of protein-ligand complexes essential. Classical techniques of structural biology include X-ray crystallography, nuclear magnetic resonance spectroscopy and recently distinguished cryo-electron microscopy. However, protein-ligand complexes are often dynamic and heterogeneous and consequently challenging for these techniques. Alternative approaches are therefore needed and gained importance during the last decades. One alternative is native mass spectrometry, which is the analysis of intact protein complexes in the gas phase. To achieve this, sample preparation and instrument conditions have to be optimised. Native mass spectrometry then reveals stoichiometry, protein interactions and topology of protein assemblies. Advanced techniques such as ion mobility and high-resolution mass spectrometry further add to the range of applications and deliver information on shape and microheterogeneity of the complexes. In this tutorial, we explain the basics of native mass spectrometry including sample requirements, instrument modifications and interpretation of native mass spectra. We further discuss the developments of native mass spectrometry and provide example spectra and applications.

Keywords: ESI; ion mobility; native MS; protein complexes; protein interactions; protein structure.

PubMed Disclaimer

References

REFERENCES

    1. Karas M, Bachmann D, Bahr U, Hillenkamp F. Matrix-assisted ultraviolet laser desorption of non-volatile compounds. Int J Mass Spectrom Ion Process. 1987;78:53-68.
    1. Tanaka K, Waki H, Ido Y, et al. Protein and polymer analyses up to m/z 100 000 by laser ionization time-of-flight mass spectrometry. Rapid Commun Mass Spectrom. 1988;2(8):151-153.
    1. Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. Electrospray ionization for mass spectrometry of large biomolecules. Science (New York, NY). 1989;246(4926):64-71.
    1. Schmidt C, Robinson CV. Dynamic protein ligand interactions-insights from MS. FEBS J. 2014;281(8):1950-1964.
    1. Mehmood S, Allison TM, Robinson CV. Mass spectrometry of protein complexes: from origins to applications. Annu Rev Phys Chem. 2015;66(1):453-474.

LinkOut - more resources