Abstract
To study the nature of antigenic recognition, antibodies have been prepared against a set of peptide sequences representing both highly mobile and well-ordered regions of myohaemerythrin, based on X-ray crystallographic temperature factors. Anti-peptide antibodies against highly mobile regions react strongly with the native protein; anti-peptide antibodies from well-ordered regions do not. Mobility is a major factor in the recognition of the native protein by anti-peptide antibodies; this may be of general significance in protein–protein interactions.
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References
Lerner, R. A. Nature 299, 592–596 (1982).
Crumpton, M. J. in The Antigens (ed. Sela, M.) 133–158 (Academic, New York, 1974).
Niman, H. L. et al. Proc. natn. Acad. Sci. U.S.A. 80, 4949–4953 (1983).
Wilson, I. A. et al. Cell 37, 767–778 (1984).
Debye, P. Ann. Phys. 43, 49 (1914).
Holbrook, S. R. & Kim, S.-H. J. molec. Biol. 173, 361–388 (1984).
Swaminathan, S., Ichiye, T., van Gunsteren, W. & Karplus, M. Biochemistry 21, 5230–5241 (1982).
Artymiuk, P. J. et al. Nature 280, 563–568 (1979).
Bernstein, F. C. et al. J. molec. Biol. 112, 535–542 (1977).
Richards, F. M. A. Rev. Biophys. Bioengng 6, 151–176 (1977).
Weber, P. C. & Salemme, F. R. Nature 287, 82–84 (1980).
Stenkamp, R. E., Sieker, L. C. & Jensen, L. H. Acta crystallogr. B 39, 697–703 (1983).
Frauenfelder, H. & Petsko, G. A. Biophys. J. 32, 465–483 (1980).
Levitt, M. J. molec. Biol. 168, 621–657 (1983).
Farr, R. S. J. infect. Dis. 103, 239–262 (1958).
Klippenstein, G. L., Van Riper, D. A. & Oosterom, E. A. J. biol. Chem. 247, 5959–5963 (1972).
McCammon, J. A. & Karplus, M. Acc. chem. Res. 16, 187–193 (1983).
Huber, R. & Bennett, W. S. Jr Biopolymers 22, 261–279 (1983).
Mao, B., Pear, M. R., McCammon, J. A. & Northrup, S. H. Biopolymers 21, 1979–1989 (1982).
Wagner, G. & Wuthrich, K. J. molec. Biol. 134, 75–94 (1979).
Benjamin, D. C. et al. A. Rev. Immun. 2, 67–101 (1984).
Chothia, C. & Janin, J. Nature 256, 705–708 (1975).
Getzoff, E. D. et al. Nature 306, 287–290 (1983).
Weiner, P. K., Langridge, R., Blaney, J. M., Schaefer, R. & Kollman, P. A. Proc. natn. Acad. Sci. U.S.A. 79, 3754–3758 (1982).
Connolly, M. L. Science 221, 709–713 (1983).
Eisenberg, D., Weiss, R. M., Terwilliger, T. C. & Wilcox, W. Faraday Symp. chem. Soc. 17, 109–120 (1982).
Green, N. et al. Cell 28, 477–487 (1982).
Johnson, D. A., Gautsch, J. W., Sportsman, J. R. & Elder, J. H. Gene analyt. Tech. 1, 3–8 (1984).
Ternynck, T. & Avranmeas, S. Immunochemistry 14, 767–774 (1977).
McConahey, P. J. & Dixon, F. J. Int. Archs Allergy appl. Immun. 29, 185–189 (1966).
Towbin, H., Staehelin, T. & Gordon, J. Proc. natn. Acad. Sci. U.S.A. 76, 4350–4354 (1979).
Connolly, M. L. J. Appl. Crystallogr. 16, 548–558 (1983).
McCammon, J. A., Wolynes, P. & Karplus, M. Biochemistry 18, 927–942 (1979).
Bondi, A. J. phys. Chem. 68, 441–451 (1964).
O'Donnell, T. J. & Olson, A. J. Comput. Graphics 15, 133–142 (1981).
Connolly, M. L. & Olson, A. J. Computers and Chemistry (in the press).
Connolly, M. L. J. molec. Graphics (in the press).
Klippenstein, G. L., Cote, J. L. & Ludlan, S. E. Biochemistry 15, 1128–1136 (1976).
Houghten, R. A., Chang, W. C. & Li, C. H. Int. J. Peptide Prot. Res. 16, 311–320 (1980).
Marglin, A. & Merrifield, R. B. A. Rev. Biochem. 39, 841–866 (1970).
Bittle, J. L. et al. Nature 298, 30–33 (1982).
Houghten, R. A. & Li, C. H. Analyt. Biochem. 98, 36–46 (1979).
Liu, F. T., Zinnecker, M., Hamaska, T. & Katz, D. H. Biochemistry 18, 690–697 (1979).
Laemmli, U. K. Nature 227, 680–685 (1970).
Sheriff, S., Hendrickson, W. A., Stenkamp, R. E., Sieker, L. C. & Jensen, L. H. Proc. natn. Acad. Sci. U.S.A. (in the press).
Westhof, E. et al. Nature 311, 123–126 (1984).
Tainer, J. A., Getzoff, E. D., Paterson, Y., Olson, A. J. & Lerner, R. A. A. Rev. Immun. (in the press).
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Tainer, J., Getzoff, E., Alexander, H. et al. The reactivity of anti-peptide antibodies is a function of the atomic mobility of sites in a protein. Nature 312, 127–134 (1984). https://doi.org/10.1038/312127a0
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DOI: https://doi.org/10.1038/312127a0
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