The charge-state model of protein polymorphism in natural populations

作者: D. R. Marshall , A. H. D. Brown

DOI: 10.1007/BF01732353

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摘要: Routine electrophoretic surveys for genetic variation in natural populations depend primarily upon detecting differences the net charge carried by a protein. We have calculated proportion of base substitutions which would yield an electrophoretically detectable mutant protein, and relative mutation rates among different classes, under variety simplifying assumptions. These calculations indicate that: (i) only 25 per cent all single mutations lead to change on protein molecule. (ii) five distinct classes variants can be generated from specified substitutions. (iii) the differ markedly substitutions. The estimates proteins were relatively robust changes assumptions concerned with kind site amino acid composition

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