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.

  • NEWS AND VIEWS

Dynamics of protein droplets revealed by bridging multiple scales

Many biological processes rely on proteins that aggregate into droplets governed by dynamics that span myriad scales. A clever combination of spectroscopy and simulation offers a way to probe these diverse dynamics.
  1. Marina G. Guenza

    1. Marina G. Guenza is in the Department of Chemistry and Biochemistry, University of Oregon, Eugene, Oregon 97403-1253, USA.

    View author publications

    You can also search for this author in PubMed  Google Scholar

Coacervates are dense protein droplets that form spontaneously in cells through a process called phase separation1. These droplets have key roles in various biological phenomena, but an understanding of the molecular-scale mechanisms through which they perform their functions remains largely elusive. This is because their macroscopic properties are intricately linked to their structure on an atomic scale. Revealing these molecular mechanisms therefore requires the investigation of properties across a wide range of time and length scales. Writing in Nature, Galvanetto et al.2 address this challenge by combining several spectroscopic techniques with computer simulations to capture the dynamics of proteins in coacervates — from their atomic movements all the way up to the fusion of phase-separated molecular droplets.

Access options

Rent or buy this article

Prices vary by article type

from$1.95

to$39.95

Learn more

Prices may be subject to local taxes which are calculated during checkout

Nature 619, 700-701 (2023)

doi: https://doi.org/10.1038/d41586-023-02215-2

References

  1. Astoricchio, E., Alfano, C., Rajendran, L., Temussi, P. A. & Pastore, A. Trends Biochem. Sci. 45, 706–717 (2020).

    Article  PubMed  Google Scholar 

  2. Galvanetto, N. et al. Nature 619, 876–883 (2023).

    Article  Google Scholar 

  3. Wright, P. E. & Dyson, H. J. Nature Rev. Mol. Cell Biol. 16, 18–29 (2015).

    Article  PubMed  Google Scholar 

  4. Shea, J. E., Best, R. B. & Mittal, J. Curr. Opin. Struct. Biol. 67, 219–225 (2021).

    Article  PubMed  Google Scholar 

  5. Alberti, S., Gladfelter, A. & Mittag, T. Cell 176, 419–434 (2019).

    Article  PubMed  Google Scholar 

  6. Lakowicz, J. R. (ed) Principles of Fluorescence Spectroscopy (Springer, 2006).

    Google Scholar 

  7. Guenza, M. G., Dinpajooh, M., McCarty, J. & Lyubimov, I. Y. J. Phys. Chem. B 122, 10257–10278 (2018).

    Article  PubMed  Google Scholar 

  8. Doi, M. & Edwards, S. F. The Theory of Polymer Dynamics (Oxford Univ. Press, 2003).

    Google Scholar 

  9. Guenza, M. J. Chem. Phys. 110, 7574–7588 (1999).

    Article  Google Scholar 

  10. Zamponi, M. et al. J. Phys. Chem. B 112, 16220–16229 (2008).

    Article  PubMed  Google Scholar 

  11. Kruteva, M. et al. Macromolecules 54, 11384–11391 (2021).

    Article  Google Scholar 

Download references

Competing Interests

The author declares no competing interests.

Subjects

Latest on:

Nature Careers

Jobs

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

Search

Advanced search

Quick links