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.
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