Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

Analytical biochemistry

Weighing up protein folding

Nature volume 468, pages 640–641 (2010)Cite this article

Subjects

Labelling molecules by fast oxidation allows mass spectrometry to study protein folding at submillisecond time resolution. The method also brings a wealth of structural information about protein folding within reach.

When it comes to protein-folding studies, mass spectrometry can provide much structural information. But its time resolution has been insufficient to detect the fastest folding events, which occur on the microsecond timescale1. Chen et al.2 now report a solution to this problem in their study of the submillisecond folding of the barstar protein, published in the Journal of the American Chemical Society. They have married two techniques that could potentially reach microsecond resolution: laser temperature jumping (T-jumping), which initiates protein-folding reactions, and fast photochemical oxidation of the protein (FPOP), which allows mass spectrometry to monitor how far folding has progressed. Their technique should enable more structural information to be obtained from studies of protein-folding kinetics — crucial for developing the next generation of computational methods for simulating protein dynamics, and to allow more complex proteins and protein complexes to be studied experimentally.

This is a preview of subscription content

Access options

Buy article

Get time limited or full article access on ReadCube.

$32.00

Buy

All prices are NET prices.

Figure 1: Improving the time resolution of mass spectrometry in protein-folding studies.

References

  1. Kubelka, J., Hofrichter, J. & Eaton, W. A. Curr. Opin. Struct. Biol. 14, 76–88 (2004).

    CAS  Article  Google Scholar 

  2. Chen, J., Rempel, D. L. & Gross, M. L. J. Am. Chem. Soc. 132, 15502–15504 (2010).

    CAS  Article  Google Scholar 

  3. Shaw, D. E. et al. Science 330, 341–346 (2010).

    ADS  CAS  Article  Google Scholar 

  4. Gruebele, M. C.R. Biol. 328, 701–712 (2005).

    CAS  Article  Google Scholar 

  5. Nölting, B., Golbik, R. & Fersht, A. R. Proc. Natl Acad. Sci. USA 92, 10668–10672 (1995).

    ADS  Article  Google Scholar 

  6. Ballew, R. M., Sabelko, J. & Gruebele, M. Proc. Natl Acad. Sci. USA 93, 5759–5764 (1996).

    ADS  CAS  Article  Google Scholar 

  7. Gau, B. C., Sharp, J. S., Rempel, D. L. & Gross, M. L. Anal. Chem. 81, 6563–6571 (2009).

    CAS  Article  Google Scholar 

  8. de Laureto, P. P., De Filippis, V., Di Bello, M., Zambonin, M. & Fontana, A. Biochemistry 34, 12596–12604 (1995).

    Article  Google Scholar 

  9. Tsui, V. et al. Protein Sci. 8, 45–49 (1999).

    CAS  Article  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Martin Gruebele is in the Departments of Chemistry and of Physics, the Center for Biophysics and Computational Biology, and at the Beckman Institute, University of Illinois, 600 South Mathews Avenue, Urbana, Illinois 61801, USA. mgruebel@illinois.edu,

    Martin Gruebele

Authors
  1. Martin Gruebele
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Gruebele, M. Weighing up protein folding. Nature 468, 640–641 (2010). https://doi.org/10.1038/468640a

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/468640a

Further reading

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

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