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 & Views
  • Published:

Structural biology

Protein self-assembly intermediates

Nature Chemical Biology volume 9, pages 216–217 (2013)Cite this article

Subjects

Proteins can self-assemble into functional states, or they can end up as aberrant and sometimes toxic aggregates. Metastable intermediate states are often detected in these processes, and their structural characterization provides vital information about the balance between functional and pathological behavior in living systems.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

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

Figure 1: Schematic view of the various metastable and stable states in protein self-assembly.

References

  1. Kim, P.S. & Baldwin, R.L. Annu. Rev. Biochem. 59, 631–660 (1990).

    Article  CAS  Google Scholar 

  2. Radford, S.E., Dobson, C.M. & Evans, P.A. Nature 358, 302–307 (1992).

    Article  CAS  Google Scholar 

  3. Kelly, J.W. Curr. Opin. Struct. Biol. 8, 101–106 (1998).

    Article  CAS  Google Scholar 

  4. Korzhnev, D.M., Religa, T.L., Banachewicz, W., Fersht, A.R. & Kay, L.E. Science 329, 1312–1316 (2010).

    Article  CAS  Google Scholar 

  5. Neudecker, P. et al. Science 336, 362–366 (2012).

    Article  CAS  Google Scholar 

  6. Jaremko, M. et al. Nat. Chem. Biol. 9, 264–270 (2013).

    Article  CAS  Google Scholar 

  7. Chiti, F. & Dobson, C.M. Nat. Chem. Biol. 5, 15–22 (2009).

    Article  CAS  Google Scholar 

  8. Cremades, N. et al. Cell 149, 1048–1059 (2012).

    Article  CAS  Google Scholar 

  9. Lindorff-Larsen, K., Best, R.B., DePristo, M.A., Dobson, C.M. & Vendruscolo, M. Nature 433, 128–132 (2005).

    Article  CAS  Google Scholar 

  10. Cavalli, A., Salvatella, X., Dobson, C.M. & Vendruscolo, M. Proc. Natl. Acad. Sci. USA 104, 9615–9620 (2007).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Michele Vendruscolo and Christopher M. Dobson are at the Department of Chemistry, University of Cambridge, Cambridge, UK.,

    Michele Vendruscolo & Christopher M Dobson

Authors
  1. Michele Vendruscolo
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Christopher M Dobson
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding authors

Correspondence to Michele Vendruscolo or Christopher M Dobson.

Ethics declarations

Competing interests

The authors declare no competing financial interests.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Vendruscolo, M., Dobson, C. Protein self-assembly intermediates. Nat Chem Biol 9, 216–217 (2013). https://doi.org/10.1038/nchembio.1210

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nchembio.1210

This article is cited by

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