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Molecular Biology and Evolution, Vol 3, 84-94, Copyright © 1986 by Society for Molecular Biology and Evolution

ORIGINAL ARTICLE

Charge changes in protein evolution

EW Peetz, G Thomson and PW Hedrick
Department of Genetics, University of California, Berkeley 94720.

The number of charge changes relative to total amino acid replacements for each of seven protein sequences (cytochrome c, hemoglobin alpha, hemoglobin beta, myoglobin, insulin, and fibrinopeptides A and B) has been studied. This number was compared with the expected value obtained under the assumption of random nucleotide substitution. The results obtained indicate that four proteins--hemoglobin alpha, hemoglobin beta, myoglobin, and insulin--are accumulating charge changes at rates slower than those predicted by a model of random substitution. Cytochrome c and fibrinopeptides A and B are accumulating charge changes at rates similar to those predicted by a random model.
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