Summary
51 polypeptides of known 3-dimensional structures have been submitted to a search for internal similarities. It is shown that the frequency of proteins displaying significant amounts of internal similarities is higher than predicted by chance. A non-negligeable part of those similarities probably occurs in connection with the existence of ordered secondary structures. Indeed, similarity occurs at a much more important rate when analyses are restricted to protein subsequences corresponding to α helices or β pleated sheets. Furthermore, the correlation existing between the rates at which linear and inverted repeats occur inside protein subregions of ordered secondary structures suggests that a significant part of short similarities are analogies rather than homologies. An hypothesis is put forward suggesting that the regular alternations of hydrophobicity which characterize most of α helices and β strands could provoke the occurrence of significant amounts of similarities inside protein sequences.
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Wuilmart, C., Delhaise, P. Linear repetitions of amino acids and convergent evolution inside protein subregions of ordered secondary structures. J Mol Evol 19, 355–361 (1983). https://doi.org/10.1007/BF02101639
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DOI: https://doi.org/10.1007/BF02101639