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
- 1
Lerner, R. A. Nature 299, 592–596 (1982).
- 2
Crumpton, M. J. in The Antigens (ed. Sela, M.) 133–158 (Academic, New York, 1974).
- 3
Niman, H. L. et al. Proc. natn. Acad. Sci. U.S.A. 80, 4949–4953 (1983).
- 4
Wilson, I. A. et al. Cell 37, 767–778 (1984).
- 5
Debye, P. Ann. Phys. 43, 49 (1914).
- 6
Holbrook, S. R. & Kim, S.-H. J. molec. Biol. 173, 361–388 (1984).
- 7
Swaminathan, S., Ichiye, T., van Gunsteren, W. & Karplus, M. Biochemistry 21, 5230–5241 (1982).
- 8
Artymiuk, P. J. et al. Nature 280, 563–568 (1979).
- 9
Bernstein, F. C. et al. J. molec. Biol. 112, 535–542 (1977).
- 10
Richards, F. M. A. Rev. Biophys. Bioengng 6, 151–176 (1977).
- 11
Weber, P. C. & Salemme, F. R. Nature 287, 82–84 (1980).
- 12
Stenkamp, R. E., Sieker, L. C. & Jensen, L. H. Acta crystallogr. B 39, 697–703 (1983).
- 13
Frauenfelder, H. & Petsko, G. A. Biophys. J. 32, 465–483 (1980).
- 14
Levitt, M. J. molec. Biol. 168, 621–657 (1983).
- 15
Farr, R. S. J. infect. Dis. 103, 239–262 (1958).
- 16
Klippenstein, G. L., Van Riper, D. A. & Oosterom, E. A. J. biol. Chem. 247, 5959–5963 (1972).
- 17
McCammon, J. A. & Karplus, M. Acc. chem. Res. 16, 187–193 (1983).
- 18
Huber, R. & Bennett, W. S. Jr Biopolymers 22, 261–279 (1983).
- 19
Mao, B., Pear, M. R., McCammon, J. A. & Northrup, S. H. Biopolymers 21, 1979–1989 (1982).
- 20
Wagner, G. & Wuthrich, K. J. molec. Biol. 134, 75–94 (1979).
- 21
Benjamin, D. C. et al. A. Rev. Immun. 2, 67–101 (1984).
- 22
Chothia, C. & Janin, J. Nature 256, 705–708 (1975).
- 23
Getzoff, E. D. et al. Nature 306, 287–290 (1983).
- 24
Weiner, P. K., Langridge, R., Blaney, J. M., Schaefer, R. & Kollman, P. A. Proc. natn. Acad. Sci. U.S.A. 79, 3754–3758 (1982).
- 25
Connolly, M. L. Science 221, 709–713 (1983).
- 26
Eisenberg, D., Weiss, R. M., Terwilliger, T. C. & Wilcox, W. Faraday Symp. chem. Soc. 17, 109–120 (1982).
- 27
Green, N. et al. Cell 28, 477–487 (1982).
- 28
Johnson, D. A., Gautsch, J. W., Sportsman, J. R. & Elder, J. H. Gene analyt. Tech. 1, 3–8 (1984).
- 29
Ternynck, T. & Avranmeas, S. Immunochemistry 14, 767–774 (1977).
- 30
McConahey, P. J. & Dixon, F. J. Int. Archs Allergy appl. Immun. 29, 185–189 (1966).
- 31
Towbin, H., Staehelin, T. & Gordon, J. Proc. natn. Acad. Sci. U.S.A. 76, 4350–4354 (1979).
- 32
Connolly, M. L. J. Appl. Crystallogr. 16, 548–558 (1983).
- 33
McCammon, J. A., Wolynes, P. & Karplus, M. Biochemistry 18, 927–942 (1979).
- 34
Bondi, A. J. phys. Chem. 68, 441–451 (1964).
- 35
O'Donnell, T. J. & Olson, A. J. Comput. Graphics 15, 133–142 (1981).
- 36
Connolly, M. L. & Olson, A. J. Computers and Chemistry (in the press).
- 37
Connolly, M. L. J. molec. Graphics (in the press).
- 38
Klippenstein, G. L., Cote, J. L. & Ludlan, S. E. Biochemistry 15, 1128–1136 (1976).
- 39
Houghten, R. A., Chang, W. C. & Li, C. H. Int. J. Peptide Prot. Res. 16, 311–320 (1980).
- 40
Marglin, A. & Merrifield, R. B. A. Rev. Biochem. 39, 841–866 (1970).
- 41
Bittle, J. L. et al. Nature 298, 30–33 (1982).
- 42
Houghten, R. A. & Li, C. H. Analyt. Biochem. 98, 36–46 (1979).
- 43
Liu, F. T., Zinnecker, M., Hamaska, T. & Katz, D. H. Biochemistry 18, 690–697 (1979).
- 44
Laemmli, U. K. Nature 227, 680–685 (1970).
- 45
Sheriff, S., Hendrickson, W. A., Stenkamp, R. E., Sieker, L. C. & Jensen, L. H. Proc. natn. Acad. Sci. U.S.A. (in the press).
- 46
Westhof, E. et al. Nature 311, 123–126 (1984).
- 47
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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