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:

Illuminating folding intermediates

Nature Structural Biology volume 7, pages 7–10 (2000)Cite this article

Abstract

Time-resolved Fourier transform infrared spectroscopy provides evidence of non-native antiparallel β-sheet structural elements in the folding intermediates of α-lactalbumin.

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

Relevant articles

Open Access articles citing this article.

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 of the folding energy landscape of a protein molecule where the energy of the protein is displayed as a function of the topological arrangements of the atoms.
Figure 2: Stereo views of the structure of α-lactalbumin (1HFZ).
Figure 3: Schematic of possible connecting reactions between the folded state, the denatured state, and the molten globule state (A-state) of α-lactalbumin.
Figure 4: Cartoon diagram of one possible idealistic representation of a transient misfolded intermediate of apo-α-lactalbumin.

References

  1. Plaxco, K.W. & Dobson, C.M. Curr. Opin. Struct. Biol. 6, 630–636 (1996).

    Article  CAS  Google Scholar 

  2. Troullier, A., Reinstädler, D., Dupont, Y., Naumann, D. & Forge, V. Nature Struct. Biol. 7 , 78–86 (2000).

  3. Gerwert, K. Curr. Opin. Struct. Biol. 3, 769–773 (1993).

    Article  CAS  Google Scholar 

  4. Troullier, A., Gerwert, K. & Dupont, Y. Biophys. J. 71, 2970– 2983 (1996).

    Article  CAS  Google Scholar 

  5. Reinstädler, D., Fabian, H., Backmann, J. & Naumann, D. Biochemistry 35, 15822–15830 (1996).

    Article  Google Scholar 

  6. Reinstädler, D., Fabian, H. & Naumann, D. Proteins 34, 303– 316 (1999).

    Article  Google Scholar 

  7. Surewicz, W.E., Mantsch, H.H. & Chapman, D. Biochemistry 32, 389– 394 (1993).

    Article  CAS  Google Scholar 

  8. Qi, X.L., Holt, C., McNulty, D., Clarke, D.T., Brownlow, S. & Jones, G.R. Biochem. J. 324, 341–346 (1997).

    Article  CAS  Google Scholar 

  9. Pappu, R.V. Proteins 36, 263–269 ( 1999).

    Article  CAS  Google Scholar 

  10. Zhou, Y. & Karplus, M. Nature 401, 400–403 (1999).

    CAS  PubMed  Google Scholar 

  11. Baldwin, R.L. J. Biomol. NMR 5, 103–109 (1995).

    Article  CAS  Google Scholar 

  12. Burton, R.E., Huang, G.S., Daugherty, M.A., Calderone, T.L. & Oas, T.G. Nature Struct. Biol. 4 , 305–310 (1997).

    Article  CAS  Google Scholar 

  13. Guijarro, J.I. et al. Biochemistry 34, 2998– 3008 (1995).

    Article  CAS  Google Scholar 

  14. Levinthal, C. J. Chim. Phys. 65, 44–45 (1968).

    Article  Google Scholar 

  15. Dobson, C.M. Nature Struct. Biol. 2, 513–517 (1995).

    Article  CAS  Google Scholar 

  16. Dill, K.A. & Chan, H.S. Nature Struct. Biol. 4, 10–19 (1997).

    Article  CAS  Google Scholar 

  17. Creighton, T.E. Protein Folding (W.H. Freeman & Company, New York, 1992).

    Google Scholar 

  18. Alm, E. & Baker D. Curr. Opin. Struct. Biol. 9, 189–196 (1999).

    Article  CAS  Google Scholar 

  19. Dobson, C.M., Sali, A. & Karplus, M. Angew. Chem. Int. Ed. 37, 868– 893 (1998).

    Article  Google Scholar 

  20. Li, R. & Woodward, C. Proteins Sci. 8, 1571–1590 (1999).

    Article  CAS  Google Scholar 

  21. Tsai, C.J., Ma, B. & Nussinov, R . Proc. Natl. Acad. Sci USA. 96, 9970–9972 (1999).

    Article  CAS  Google Scholar 

  22. Qasba, P.K. & Kumar, S. Crit. Rev. Biochem. Mol. Biol. 32, 255–306 (1997).

    Article  CAS  Google Scholar 

  23. Pike, A.C., Brew, K. & Acharya, K.R. Structure 4, 691– 703 (1996).

    Article  CAS  Google Scholar 

  24. Sugai, S. & Ikeguchi, M. Adv. Biophys. 30, 37–84 (1994).

    Article  CAS  Google Scholar 

  25. Veprintsev, D.M. et al. FEBS Lett. 412, 625– 628 (1997).

    Article  CAS  Google Scholar 

  26. Wu, L.C., Peng, Z.-Y. & Kim, P.S. Nature Struct. Biol. 2, 281– 286 (1995).

    Article  CAS  Google Scholar 

  27. Ptitsyn, O. Nature Struct. Biol. 3, 488–490 (1996).

    Article  CAS  Google Scholar 

  28. Creighton, T. Trends Biochem. Sci. 22, 6–10 (1997).

    Article  CAS  Google Scholar 

  29. Demarest, S.J., Boice, J.A., Fairman, R. & Raleigh, D.P. J. Mol. Biol. 294, 213–221 ( 1999).

    Article  CAS  Google Scholar 

  30. Wu, L.C. & Kim, P.S. J. Mol. Biol. 280, 175–182 (1998).

    Article  CAS  Google Scholar 

  31. Fabian, H. & Mantsch, H.H. Biochemistry 34, 13651–13655 (1995).

    Article  CAS  Google Scholar 

  32. Noda, I. Applied Spectroscopy 47, 1329–1336 (1993).

    Article  CAS  Google Scholar 

  33. Fabian, H., Mantsch, H.H. & Schultz, C.P. Proc. Natl. Acad. Sci. USA 96, 13153–13158 (1999).

    Article  CAS  Google Scholar 

  34. Sonar, S. et al. Nature Struct. Biol. 1, 512– 517 (1994).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Biomedical Applications, Bruker Optics, Billerica, 01821 , Massachusetts, USA

    Christian P. Schultz

Authors
  1. Christian P. Schultz
    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

Schultz, C. Illuminating folding intermediates. Nat Struct Mol Biol 7, 7–10 (2000). https://doi.org/10.1038/71197

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/71197

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