Charge changes in protein evolution

E. W. Peetz, G. Thomson, P. W. Hedrick

Research output: Contribution to journalArticle

4 Scopus citations


The number of charge changes relative to total amino acid replacements for each of seven protein sequences (cytochrome c, hemoglobin α, hemoglobin β, 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 α, hemoglobin β, 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.

Original languageEnglish (US)
Pages (from-to)84-94
Number of pages11
JournalMolecular Biology and Evolution
Issue number1
Publication statusPublished - 1986
Externally publishedYes


ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Ecology, Evolution, Behavior and Systematics
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Genetics
  • Molecular Biology
  • Genetics(clinical)

Cite this

Peetz, E. W., Thomson, G., & Hedrick, P. W. (1986). Charge changes in protein evolution. Molecular Biology and Evolution, 3(1), 84-94.