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.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Perutz, M. F., Kendrew, J. C. & Watson, H. C. J. molec. Biol. 13, 669–678 (1965).
Schiffer, M. & Edmundson, A. B. Biophys. J. 7, 121–135 (1967).
Morrisett, J. D., Jackson, R. L. & Gotto, A. M. Jr Biochim. biophys. Acta 472, 93–133 (1977).
Segrest, J. P., Jackson, R. L., Morrisett, J. D. & Gotto, A. M. Jr FEBS Lett. 38, 247–253 (1974).
Segrest, J. P. & Feldman, R. J. Biopolymers 16, 2053–2065 (1977).
DeGrado, W. F., Kezdy, F. J. & Kaiser, E. T. J. Am. chem. Soc. 103, 679–681 (1981).
Ptitsyn, O. B. & Rashin, A. A. Biophys. Chem. 3, 1–20 (1975).
Janin, J. Nature 277, 491–492 (1979).
Wolfenden, R., Andersson, L., Cullis, P. M. & Southgate, C. C. B. Biochemistry 20, 849–855 (1981).
von Heijne, G. & Blomberg, C. Eur. J. Biochem. 97, 175–181 (1979).
Chothia, C. J. molec. Biol. 105, 1–14 (1976).
Segrest, J. P. & Feldman, R. J. J. molec. Biol. 87, 853–858 (1974).
Henderson, R. Soc. gen. Physiol. 33, 3–15 (1979).
Feldman, R. J. Atlas of Macromolecular Structure on Microfiche (Tracer Jitco, Rockville, Maryland, 1976).
Habermann, E. Science 177, 314–322 (1972).
Kriel, G. FEBS Lett. 33, 241–244 (1973).
Fitton, J. E., Dell, A. & Shaw, W. V. FEBS Lett. 115, 209–212 (1980).
Terwilliger, T. C. & Eisenberg, D. J. biol. Chem. 257, 6016–6022 (1982).
Terwilliger, T. C., Weissman, L. & Eisenberg, D. Biophys. J. 37, 353–361 (1982).
Kayser, G. et al. Biochem. biophys. Res. Commun. 99, 358–363 (1981).
Engelman, D. M., Henderson, R., McLachlan, A. D. & Wallace, B. A. Proc. natn. Acad. Sci. U.S.A. 77, 2023–2027 (1980).
Wilson, I. A., Wiley, D. C. & Skehel, J. J. Nature 289, 366–373 (1981).
Porter, A. G. et al. Nature 282, 471–477 (1979).
Bloomer, A. C., Champness, J. N., Bricogne, G., Staden, R. & Klug, A. Nature 276, 362–368 (1978).
Dayhoff, M. O. Atlas of Protein Sequence and Structure Vol. 5, D283 (National Biomedical Research Foundation, Washington DC, 1972).
Furthmayr, H., Galardy, R. E., Tomita, M. & Marchesi, V. T. Archs Biochem. Biophys. 185, 21–29 (1978).
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).
Verhoeyen, M. et al. Nature 286, 771–776 (1980).
Rogers, J. et al. Cell 20, 303–312 (1980).
Frank, G. et al. FEBS Lett. 96, 183–188 (1978).
Wickner, W. Science 210, 861–868 (1980).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
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
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/299371a0
This article is cited by
-
Interaction of designed cationic antimicrobial peptides with the outer membrane of gram-negative bacteria
Scientific Reports (2024)
-
A novel designed membrane-active peptide for the control of foodborne Salmonella enterica serovar Typhimurium
Scientific Reports (2023)
-
Effect of hydrophobic moment on membrane interaction and cell penetration of apolipoprotein E-derived arginine-rich amphipathic α-helical peptides
Scientific Reports (2022)
-
Viral Prefusion Targeting Using Entry Inhibitor Peptides: The Case of SARS-CoV-2 and Influenza A virus
International Journal of Peptide Research and Therapeutics (2022)
-
Unravelling the molecular effect of ocellatin-1, F1, K1 and S1, the frog-skin antimicrobial peptides to enhance its therapeutics—quantum and molecular mechanical approaches
Journal of Molecular Modeling (2021)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.