News & Views | Published:

Mass spectrometry

Raw protein from the top down

Nature Chemistry volume 10, pages 114116 (2018) | Download Citation

Mass spectrometry is a powerful technique for analysing proteins, yet linking higher-order protein structure to amino acid sequence and post-translational modifications is far from simple. Now, a native top-down method has been developed that can provide information on higher-order protein structure and different proteoforms at the same time.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1.

    , & Nat. Rev. Genet. 14, 35–48 (2013).

  2. 2.

    & Nature 537, 347–355 (2016).

  3. 3.

    , , , & Nat. Chem. 10, 139–148 (2018).

  4. 4.

    , & The Consortium for Top Down Proteomics Nat. Methods 10, 186–187 (2013).

  5. 5.

    , & Biochem. Biophys. Res. Commun. 445, 683–693 (2014).

  6. 6.

    Anal. Chem. 88, 30–51 (2016).

  7. 7.

    Int. J. Mass Spectrom. 200, 175–186 (2000).

  8. 8.

    & Annu. Rev. Biochem. 76, 167–193 (2007).

  9. 9.

    & Protein Sci. 24, 1176–1192 (2015).

  10. 10.

    , & R. EMBO J. 35, 2634–2657 (2016).

  11. 11.

    & Proc. Natl Acad. Sci. USA 105, 18145–18152 (2008).

  12. 12.

    et al. Nat. Chem. Biol. 14, 36–41 (2018).

Download references

Author information

Affiliations

  1. Kathrin Breuker is in the Institute of Organic Chemistry and the Center for Molecular Biosciences Innsbruck (CMBI) at the University of Innsbruck, Innrain 80/82, 6020 Innsbruck, Austria

    • Kathrin Breuker

Authors

  1. Search for Kathrin Breuker in:

Corresponding author

Correspondence to Kathrin Breuker.

About this article

Publication history

Published

DOI

https://doi.org/10.1038/nchem.2936

Newsletter Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing