The helical hydrophobic moment: a measure of the amphiphilicity of a helix (original) (raw)

Nature volume 299, pages 371–374 (1982)Cite this article

Abstract

The spatial distribution of the hydrophobic side chains in globular proteins is of considerable interest. It was recognized previously1 that most of the _α_-helices of myoglobin and haemoglobin are amphiphilic; that is, one surface of each helix projects mainly hydrophilic side chains, while the opposite surface projects mainly hydrophobic side chains. To quantify the amphiphilicity of a helix, here we define the mean helical hydrophobic moment, 〈μH〉 = |ΣNi=1 H⇀i/N, to be the mean vector sum of the hydrophobicities H⇀i of the side chains of a helix of N residues. The length of a vector H⇀i is the signed numerical hydrophobicity associated with the type of side chain, and its direction is determined by the orientation of the side chain about the helix axis. A large value of 〈μH〉 means that the helix is amphiphilic perpendicular to its axis. We have classified _α_-helices by plotting their mean helical moment versus the mean hydrophobicity of their residues, and report that trans-membrane helices, helices from globular proteins and helices which are believed to seek surfaces between aqueous and non-polar phases, cluster in different regions of such a plot. We suggest that this classification may be useful in identifying helical regions of proteins which bind to the surface of biological membranes. The concept of the hydrophobia moment can be generalized also to non-helical protein structures.

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References

  1. Perutz, M. F., Kendrew, J. C. & Watson, H. C. J. molec. Biol. 13, 669–678 (1965).
    Article CAS Google Scholar
  2. Schiffer, M. & Edmundson, A. B. Biophys. J. 7, 121–135 (1967).
    Article CAS Google Scholar
  3. Morrisett, J. D., Jackson, R. L. & Gotto, A. M. Jr Biochim. biophys. Acta 472, 93–133 (1977).
    Article CAS Google Scholar
  4. Segrest, J. P., Jackson, R. L., Morrisett, J. D. & Gotto, A. M. Jr FEBS Lett. 38, 247–253 (1974).
    Article CAS Google Scholar
  5. Segrest, J. P. & Feldman, R. J. Biopolymers 16, 2053–2065 (1977).
    Article CAS Google Scholar
  6. DeGrado, W. F., Kezdy, F. J. & Kaiser, E. T. J. Am. chem. Soc. 103, 679–681 (1981).
    Article CAS Google Scholar
  7. Ptitsyn, O. B. & Rashin, A. A. Biophys. Chem. 3, 1–20 (1975).
    Article CAS Google Scholar
  8. Janin, J. Nature 277, 491–492 (1979).
    Article ADS CAS Google Scholar
  9. Wolfenden, R., Andersson, L., Cullis, P. M. & Southgate, C. C. B. Biochemistry 20, 849–855 (1981).
    Article CAS Google Scholar
  10. von Heijne, G. & Blomberg, C. Eur. J. Biochem. 97, 175–181 (1979).
    Article CAS Google Scholar
  11. Chothia, C. J. molec. Biol. 105, 1–14 (1976).
    Article CAS Google Scholar
  12. Segrest, J. P. & Feldman, R. J. J. molec. Biol. 87, 853–858 (1974).
    Article CAS Google Scholar
  13. Henderson, R. Soc. gen. Physiol. 33, 3–15 (1979).
    CAS Google Scholar
  14. Feldman, R. J. Atlas of Macromolecular Structure on Microfiche (Tracer Jitco, Rockville, Maryland, 1976).
    Google Scholar
  15. Habermann, E. Science 177, 314–322 (1972).
    Article ADS CAS Google Scholar
  16. Kriel, G. FEBS Lett. 33, 241–244 (1973).
    Article Google Scholar
  17. Fitton, J. E., Dell, A. & Shaw, W. V. FEBS Lett. 115, 209–212 (1980).
    Article CAS Google Scholar
  18. Terwilliger, T. C. & Eisenberg, D. J. biol. Chem. 257, 6016–6022 (1982).
    CAS PubMed Google Scholar
  19. Terwilliger, T. C., Weissman, L. & Eisenberg, D. Biophys. J. 37, 353–361 (1982).
    Article CAS Google Scholar
  20. Kayser, G. et al. Biochem. biophys. Res. Commun. 99, 358–363 (1981).
    Article CAS Google Scholar
  21. Engelman, D. M., Henderson, R., McLachlan, A. D. & Wallace, B. A. Proc. natn. Acad. Sci. U.S.A. 77, 2023–2027 (1980).
    Article ADS CAS Google Scholar
  22. Wilson, I. A., Wiley, D. C. & Skehel, J. J. Nature 289, 366–373 (1981).
    Article ADS CAS Google Scholar
  23. Porter, A. G. et al. Nature 282, 471–477 (1979).
    Article ADS CAS Google Scholar
  24. Bloomer, A. C., Champness, J. N., Bricogne, G., Staden, R. & Klug, A. Nature 276, 362–368 (1978).
    Article ADS CAS Google Scholar
  25. Dayhoff, M. O. Atlas of Protein Sequence and Structure Vol. 5, D283 (National Biomedical Research Foundation, Washington DC, 1972).
    Google Scholar
  26. Furthmayr, H., Galardy, R. E., Tomita, M. & Marchesi, V. T. Archs Biochem. Biophys. 185, 21–29 (1978).
    Article CAS Google Scholar
  27. Rose, J. K., Welch, W. J., Sefton, B. M., Esch, F. S. & Ling, N. C. Proc. natn. Acad. Sci. U.S.A. 77, 3884–3888 (1980).
    Article ADS CAS Google Scholar
  28. Verhoeyen, M. et al. Nature 286, 771–776 (1980).
    Article ADS CAS Google Scholar
  29. Rogers, J. et al. Cell 20, 303–312 (1980).
    Article CAS Google Scholar
  30. Frank, G. et al. FEBS Lett. 96, 183–188 (1978).
    Article CAS Google Scholar
  31. Wickner, W. Science 210, 861–868 (1980).
    Article ADS CAS Google Scholar

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Authors and Affiliations

  1. Molecular Biology Institute and Department of Chemistry, University of California at Los Angeles, Los Angeles, California, 90024, USA
    David Eisenberg, Robert M. Weiss & Thomas C. Terwilliger

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  1. David Eisenberg
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  2. Robert M. Weiss
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  3. Thomas C. Terwilliger
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Eisenberg, D., Weiss, R. & Terwilliger, T. The helical hydrophobic moment: a measure of the amphiphilicity of a helix.Nature 299, 371–374 (1982). https://doi.org/10.1038/299371a0

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