The Amino-acid Sequence of Cytochrome c from Euglena gracilis

THE large number of mitochondrial cytochrome c sequences known and the elucidation of the tertiary structure of the horse heart protein by Dickerson's group1 provide a good opportunity for studying the evolution of a molecule and for correlating structure with function. Dickerson has shown that relating sequence data to the tertiary structure can generate hypotheses about functional regions that are evolutionarily conserved. There is no general agreement, however, as to whether the differences in sequence from different species are adaptive or neutral and this is an aspect of the current selectionist versus neutralist argument2.

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