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By using a combination of evolutionary and structural data from 231 species, we have addressed the relationship between evolution and structural features of cytochrome b and COX I, two mtDNA-encoded proteins. The interior of cytochrome b, in contrast to that of COX I, exhibits a remarkable tolerance to changes. The higher evolvability of cytochrome b contrasts with the lower rate of synonymous substitutions of its gene when compared to that of COX I, suggesting that the latter is subjected to a stronger purifying selection. We present evidences that the stability effect of mutations (ΔΔG) may be behind these differential behaviour.


Juan Carlos Aledo, Héctor Valverde, Manuel Ruíz-Camacho. Thermodynamic stability explains the differential evolutionary dynamics of cytochrome b and COX I in mammals. Journal of molecular evolution. 2012 Feb;74(1-2):69-80

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PMID: 22362464

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