Abstract
BIOLOGICAL properties of proteins depend on the higher levels of their structure, determined by the primary structure. As has been shown by Fisher1, the knowledge of the amino-acid composition permits in many cases the tertiary and sometimes the quaternary structure of the proteins to be predicted. The ratio of the polar and non-polar amino-acids seems to be a very important characteristic of the protein. The change of the relative numbers of the polar and non-polar amino-acids as a result of a mutation must produce big changes in the protein structure. The mutational exchange of a polar group for a non-polar one and vice versa must be more dangerous than the transition from one polar group to another or from a non-polar to another non-polar one. The well-known example is the transition from Glu to Val in the case of sickle-cell haemoglobin.
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References
Fisher, H. F., Proc. U.S. Nat. Acad. Sci., 51, 1285 (1964).
Nirenberg, M. W., et al., Cold Spring Harbor Symp., 28, 549 (1963).
Speyer, J. F., et al., Cold Spring Harbor Symp., 28, 559 (1963).
Freese, E., in Molecular Genetics, Part 1, edit. by Taylor, J. H. (Academic Press, 1963).
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VOLKENSTEIN, M. Coding of Polar and Non-polar Amino-acids. Nature 207, 294–295 (1965). https://doi.org/10.1038/207294a0
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DOI: https://doi.org/10.1038/207294a0
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