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.

  • Insight
  • Published:

Helix packing angle preferences

Abstract

The distribution of interaxial angles between packed α-helices has been explained by a number of elegant models describing how side chains on helices can interdigitate without steric conflicts. Here I show that much of the apparent preference for particular angles is due to statistical bias and that true packing angle preferences are not well described by regular packing models.

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

Access options

Buy this article

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

References

  1. Chothia, C., Levitt, M. & Richardson, D. Helix to helix packing in proteins. J. Mol. Biol. 145, 215–250 (1981).

    Article  CAS  Google Scholar 

  2. Walther, D., Eisenhaber, F. & Argos, P. Principles of helix-helix packing in proteins: the helical lattice superposition model. J. Mol. Biol. 25, 536–553 (1996).

    Article  Google Scholar 

  3. Chothia, C., Levitt, M. & Richardson, D. Structure of proteins: packing of α-helices and pleated sheets. Proc. Natl. Acad. Sci., USA 74, 4130–4134 (1977).

    Article  CAS  Google Scholar 

  4. Richmond, T. & Richards, F. Packing of α-helices: geometrical constraints and contact areas. J. Mol. Biol. 119, 537–555 (1978).

    Article  CAS  Google Scholar 

  5. Reddy, B. & Blundell, T. Packing of secondary structural elements in proteins. Analysis and prediction of inter-helix distances. J. Mol. Biol. 233, 464–479 (1993).

    Article  CAS  Google Scholar 

  6. Crick, F. The packing of α-helices: simple coiled coils. Acta Crystallogr. 6, 689–697 (1953).

    Article  CAS  Google Scholar 

  7. Effimov, A. Packing of α-helices in globular proteins. Layer-structure of globin hydrophobic cores. J. Mol. Biol. 134, 23–40 (1979).

    Article  Google Scholar 

  8. O'Shea, E., Klemm, J., Kim, P. & Alber, T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254, 539–544 (1991).

    Article  CAS  Google Scholar 

  9. Bowie, J. Helix packing in membrane proteins. J. Mol. Biol. 272, 780–789 (1997).

    Article  CAS  Google Scholar 

  10. Hobohm, U. & Sander, C. Enlarged representative set of protein structures. Prot. Sci. 3, 522 (1994).

    Article  CAS  Google Scholar 

  11. Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577–2637 (1983).

    Article  CAS  Google Scholar 

  12. Shrake, A. & Rupley, J. Environment and exposure to solvent of protein atoms, lysozyme and insulin. J. Mol. Biol. 79, 351–371 (1973).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to James U. Bowie.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Bowie, J. Helix packing angle preferences. Nat Struct Mol Biol 4, 915–917 (1997). https://doi.org/10.1038/nsb1197-915

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nsb1197-915

This article is cited by

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