Abstract
THE ever-increasing amount of comparative sequence data confirms that, in general, each protein evolves at a specific, more or less constant rate1–3 . The rate of acceptance mutations in a particular gene is apparently influenced by the biological role and the size of the corresponding protein2. Knowledge of the rate and pattern of amino acid substitutions in more and functionally diverse proteins is, however, required to understand better the principles governing the evolution proteins. It is moreover important to determine which residues in a given polypeptide chain are constant throughout evolution, because they can be considered to be of vital importance for the appropriate functioning of that protein.
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DE JONG, W., VAN AMELSVOORT, J., VAN DER OUDERAA, F. et al. Slow Rate of Evolution of αA Chain of α-Crystallin. Nature New Biology 246, 233–236 (1973). https://doi.org/10.1038/newbio246233a0
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DOI: https://doi.org/10.1038/newbio246233a0
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