title: Charge changes in protein evolution.
abstract: 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.
authors.affiliation: Department of Genetics, University of California, Berkeley 94720.
authors.forename: E W
authors.initials: EW
authors.lastname: Peetz
authors.forename: G
authors.initials: G
authors.lastname: Thomson
authors.forename: P W
authors.initials: PW
authors.lastname: Hedrick
mesh_terms: D000818:Animals; D005075:Biological Evolution; D003574:Cytochrome c Group; D005344:Fibrinopeptide A; D005345:Fibrinopeptide B; D006454:Hemoglobins; D006801:Humans; D007328:Insulin; D007526:Isoelectric Point; D009211:Myoglobin; D011506:Proteins
chemical_list: D003574:Cytochrome c Group; D006454:Hemoglobins; D007328:Insulin; D009211:Myoglobin; D011506:Proteins; D005344:Fibrinopeptide A; D005345:Fibrinopeptide B