Convenient Asymmetric Unit for Construction of Multi-subunit Models


THE striking symmetry of the arrangement of protein subunits in multi-subunit enzymes and in viruses has been amply demonstrated in recent years1. Caspar2,3 pointed out that symmetry is to be expected in any self-assembling system stabilized by multiple weak interactions (that is, where the final structure is thermodynamically determined) and that it merely ensures the formation of the maximum number of stable bonds between identical units. The possible functional significance of such symmetrical arrangements has been considered in detail by Monod, Wyman and Changeux4 in their provocative interpretation of allosteric effects and cooperative binding.

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    Reed, L. J., and Cox, D. J., Ann. Rev. Biochem., 35, 57 (1966).

  2. 2

    Caspar, D. L. D., Advances in Protein Chem., 18, 37 (1963).

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    Caspar, D. L. D., in Principles of Biomolecular Organization, Ciba Foundation Symp. (J. and A. Churchill, 1966).

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    Monod, J., Wyman, J., and Changeux, J. P., J. Mol. Biol., 12, 88 (1965).

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    Valentine, R. C., and Chignell, D. A., Nature, 218, 950 (1968).

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    Klug, A., Crick, F. H. C., and Wyckoff, H. W., Acta Cryst., 11, 199 (1958).

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    Pauling, L., Discussions of the Faraday Society, No. 13, 170 (1953).

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