Abstract
IT is generally accepted that evolution of proteins is a consequence of duplications and point mutations occurring in genes coding for them. Palaeogenetics of Pauling and Zuckerkandl1 as well as protein phylogenetics introduced by Fitch and Margoliash2 (and subsequently modified by other workers) assume that comparative analyses of amino acid sequence data in terms of mutational distances (be it minimal mutational distances, corrected mutational distances or accepted point mutations per 100 amino acids), inferred to exist among genes coding for them, yield a realistic image of evolution; thus, genealogical trees of proteins (that is, dendrograms of mutational distances) can be constructed which relate to main evolutionary events thought to occur in the past.
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NOVOTNÝ, J., FRANĚK, F. Different degrees of interspecies homology in immunoglobulin λ chain constant domain correlated with three-dimensional structure. Nature 258, 641–643 (1975). https://doi.org/10.1038/258641a0
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DOI: https://doi.org/10.1038/258641a0
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