Abstract
I RE-EXAMINE here the recently published empirical equations of Chothia1 for the accessible surface area of 12 monomeric proteins, and demonstrate that accessible surface area of monomeric proteins varies as the 2/3 power of the molecular weight. The total packing volumes of proteins are obtained from the sum of the individual residues, and the approximation of proteins as spheres is used to predict the loss of accessible surface on association of two proteins. The treatment is extended to calculate the proportion of the monomer surface buried in the formation of higher oligomers.
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References
Chothia, C., Nature, 254, 304–308 (1975).
McMeekin, T. L., Groves, M. L., and Hipp, N. J., J. Am. chem. Soc., 71, 3298–3300 (1949).
Richards, F. M., J. molec. Biol., 82, 1–14, (1974).
Chothia, C., and Janin, J., Nature, 256, 705–708 (1975).
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TELLER, D. Accessible area, packing volumes and interaction surfaces of globular proteins. Nature 260, 729–731 (1976). https://doi.org/10.1038/260729a0
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DOI: https://doi.org/10.1038/260729a0
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