Abstract
A simple diagrammatic representation has been used to show the arrangement of α helices and β sheets in 31 globular proteins, which are classified into four clearly separated classes. The observed arrangements are significantly non-random in that pieces of secondary structure adjacent in sequence along the polypeptide chain are also often in contact in three dimensions.
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References
Schulz, G. E., and Schirmer, R. H., Nature, 250, 144–145 (1974).
Rossman, M. G., Moras, D., and Olsen, K. W., Nature, 250, 194–199 (1974).
Hendrickson, W. A., Klipperstein, G. L., and Ward, K. B., Proc. natn. Acad. Sci. U.S.A., 72, 2160–2164 (1975).
Kretsinger, R. H., and Nuckolds, C. E., J. biol. Chem., 248, 3313–3326 (1973).
Kendrew, J. C., Dickerson, R. E., Strandberg, B. E., Hart, R. G., and Davies, D. R., Nature, 185, 422–425 (1960).
Watson, H. C., in Prog. Stereochem., 4, 299–333 (1960).
Watenpaugh, K. D., Sieker, L. C., Herriott, J. R., and Jensen, L. H., Acta Crystallogr., B 29, 943–956 (1973).
Schiffer, M., Girling, R. L., Ely, K. R., and Edmundson, A. B., Biochemistry, 12, 4620–4631 (1973).
Poljak, R. J., et al., Proc. natn. Acad. Sci. U.S.A., 70, 3305–3310 (1973).
Segal, D. M., et al., Proc. natn. Acad. Sci. U.S.A., 71, 4298–4302 (1974).
Epp, C., et al., Eur. J. Biochem., 45, 513–524 (1974).
Blake, C. C. F., Geisow, M. J., Swan, I. D. A., Rerat, C., and Rerat, B., J. molec. Biol., 88, 1–12 (1974).
Richardson, J. S., Thomas, K. A., Rubin, B. H., and Richardson, D. C., Proc. natn. Acad. Sci. U.S.A., 72, 1349–1353 (1975).
Edelman, G. M., et al., Proc. natn. Acad. Sci. U.S.A., 69, 2580–2584 (1972).
Hardman, K. D., and Ainsworth, C. F., Biochemistry, 11, 4910–4919 (1972).
Birktoft, J. J., Blow, D. M., Henderson, R., and Steitz, T. A., Proc. R. Soc., B 257, 67–76 (1970).
Birktoft, J. J., and Blow, D. M., J. molec. Biol., 68, 187–240 (1972).
Adams, M. J., et al., Nature, 224, 491–495 (1969).
Huber, R., Kukla, D., Ruhlmann, A., and Steigemann, W., in Proc. Int. Res. Conf. Proteinase Inhibitors, Munich 1970 (edit. by Fritz, H., and Tschesche, H.), 56–64 (de Gruyter, Berlin, 1970).
Mathews, F. S., Levine, M., and Argos, P., Nature new Biol., 233, 15–16 (1971).
Wyckoff, H. W., et al., J. biol. Chem., 245, 305–328 (1970).
Blake, C. C. F., Mair, G. A., North, A. C. T., Phillips, D. C., and Sarma, V. R., Proc. R. Soc., B 167, 365–385 (1967).
Arnone, A., et al., J. biol. Chem., 246, 2302–2316 (1971).
Matthews, B. W., and Remington, S. J., Proc. natn. Acad. Sci. U.S.A., 71, 4178–4182 (1975).
Drenth, J., Jansonius, J. M., Koekoek, R., and Wolthers, B. G., Adv. Protein Chem., 25, 79–115 (1971).
Colman, P. M., Jansonius, J. N., and Matthews, B. W., J. molec. Biol., 70, 701–724 (1972).
Holmgren, A., Soderberg, B. -O., Elkund, H., and Branden, C. -I., Proc. natn. Acad. Sci. U.S.A., 72, 2307–2309 (1975).
Watenpaugh, K. D., Sieker, L. C., Jensen, L. H., Legall, J., and Dubourdieu, M., Proc. natn. Acad. Sci. U.S.A., 69. 3185–3188 (1972).
Anderson, R. D., Proc. natn. Acad. Sci. U.S.A., 69, 3189–3191 (1972).
Branden, C. I., et al., Proc. natn. Acad. Sci. U.S.A., 70, 2439–2442 (1973).
Campbell, J. W., Watson, H. C., and Hodgson, G. I., Nature, 250, 301–303 (1974).
Schulz, G. E., Elzinga, M., Marx, F., and Schirmer, R. H., Nature, 250, 120–123 (1974).
Banner, D. W., et al., Nature, 255, 609–614 (1975).
Wright, C. S., Alden, R. A., and Kraut, J., Nature, 221, 235–242 (1969).
Quiocho, F. A., and Lipscomb, W. N., Adv. Protein Chem., 25, 1–78 (1971).
Adams, M. J., Ford, G. C., Liljas, A., and Rossmann, M. G., Biochem. biophys. Res. Commun., 53, 46–51 (1973).
Blake, C. C. F., and Evans, P. R., J. molec. Biol., 84, 585–603 (1974).
Blake, C. C. F., in Essays in Biochemistry, 11, 37–79 (edit. by Campbell, P. N. and Aldridge, W. N.) (Academic, London 1975).
Buehner, M., Ford, G. C., Moras, D., Olsen, K. W., and Rossmann, M. G., Proc. natn. Acad. Sci. U.S.A., 70, 3052–3054 (1973).
Fletterick, R. J., Bates, D. J., and Steitz, T. A., Proc. natn. Acad. Sci. U.S.A., 72, 38–42 (1975).
Stroud, R. M., Kay, L. M., and Dickerson, R. E., J. molec. Biol., 83, 185–208 (1974).
Shotton, D. M., and Watson, H. C., Nature, 225, 811–816 (1970).
Perutz, M. F., et al., Nature, 222, 1240–1244 (1968).
Baldwin, J. M., prog. Biophys. molec. Biol., 29, 225–320 (1975).
Carter, C. W., Jr, et al., J. biol. Chem., 249, 4212–4225 (1974).
Salemme, F. R., et al., J. biol. Chem., 248, 3910–3921 (1973).
Hill, E., Tsernoglou, Webb, L., and Banaszak, L. J., J. molec. Biol., 72, 577–591 (1972).
Adman, E. T., Sieker, L. C., and Jensen, L. H., J. biol. Chem., 248, 3987–3996 (1973).
Bergsma, J., et al., J. molec. Biol., 98, 637–643 (1965).
Kannan, K. K., et al., Cold Spring Harb. Symp. quant. Biol., 36, 221–231 (1971).
Sweet, R. M., Wright, H. T., Chothia, C. H., and Blow, D. M., Biochemistry, 13, 4213–4228 (1974).
Champness, J. N., et al., Nature, 259, 20–24 (1976).
Holmes, K. C., Stubbs, G. J., Mandelkow, E., and Gallwitz, U., Nature, 254, 192–196 (1975).
Henderson, R., and Unwin, P. N. T., Nature, 257, 28–32 (1975).
Rao, S. T., and Rossmann, M. G., J. molec. Biol., 76, 241–256 (1973).
Karplus, M., and Weaver, D. L., Nature, 260, 404–406 (1976); Sternberg, M. J. E., and Thornton, J. M., J. molec. Biol. (in the press).
Richardson, J. S., Richardson, D. C., Thomas, K. A., Silverton, E. W., and Davies, D. R., J. molec. Biol., 102, 221–235 (1976).
Phillips, D. C., Proc. natn. Acad. Sci. U.S.A., 57, 484–495 (1967).
Goldberg, M. E., J. molec. Biol., 46, 441–446 (1969).
Veron, M., Falcoz-Kelly, F., and Cohen, G. N., Eur. J. Biochem., 28, 520–527 (1972).
Light, A., Taniuchi, H., and Chen, R. F., J. biol. Chem., 249, 2285–2299 (1974).
Ptitsyn, O. B., and Rashin, A. A., Biophys. Chem., 3, 1–20 (1974).
Wetlaufer, D. E., Proc. natn. Acad. Sci. U.S.A., 70, 697–701 (1974).
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Levitt, M., Chothia, C. Structural patterns in globular proteins. Nature 261, 552–558 (1976). https://doi.org/10.1038/261552a0
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DOI: https://doi.org/10.1038/261552a0
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