Charge changes in protein evolution

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

Research output: Contribution to journalArticlepeer-review

6 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
StatePublished - 1986
Externally publishedYes

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics
  • Molecular Biology
  • Genetics


Dive into the research topics of 'Charge changes in protein evolution'. Together they form a unique fingerprint.

Cite this