title: The charge-state model of protein polymorphism in natural populations.
abstract: Routine electrophoretic surveys for genetic variation in natural populations depend primarily upon detecting differences in the net charge carried by a protein. We have calculated the proportion of base substitutions which would yield an electrophoretically detectable mutant protein, and the relative mutation rates among different chare classes, under a variety of simplifying assumptions. These calculations indicate that: (i) only 25 per cent of all single base mutations would lead to a charge change on a protein molecule. (ii) five distinct classes of electrophoretic variants can be generated from a specified protein by single base substitutions. (iii) the relative mutation rates differ markedly among the different charge classes which can be generated by single base substitutions. The estimates of the proportion of electrophoretically detectable mutant proteins and relative mutation rates among charge classes were relatively robust to changes in assumptions concerned with the kind and site of base substitutions and the amino acid composition of the protein.
mesh_terms: D000483:Alleles; D000596:Amino Acids / Q000032:analysis; D005075:Biological Evolution; D003062:Codon; D004563:Electrochemistry; D004586:Electrophoresis; D014644:Genetic Variation; D008954:Models, Biological; D009154:Mutation; D011110:Polymorphism, Genetic; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis
chemical_list: D000596:Amino Acids; D003062:Codon; D011506:Proteins