Journal de phylogénétique et de biologie évolutive

Amino-Acid Correlated Mutations inside a Single Protein System: A New Method for the Identification of Main Coherent Directions of Evolutive Changes

Abstract

Alessandro Giuliani, Roberto Bruni, Massimo Ciccozzi, Alessandra Lo Presti, Michele Equestre, Cinzia Marcantonio and Anna Rita Ciccaglione

The need of giving rise to a stable and soluble protein system generates constraints that limit the mutation space by imposing a co-variation structure across different residues. While protein scientists widely use this property in order to predict protein-protein interaction and peptide-receptor pairing, there is no equivalent interest to make use of mutation correlation structures to get information inside single protein systems. Here we present a methodological essay that, using a statistical approach typical of medicinal chemistry, faces the problem to locate ‘mutational correlation units’ in a viral RNA polymerase. These ‘units’ are invisible to ordinary sequence alignment methods and can be important in virus characterization and vaccine developments as well as for evolution theorists.