Andrea Pagnani — Politecnico di Torino #
Exploiting co-evolution across protein families for predicting protein-protein interaction #
Correlated substitution patterns between residues of a protein family have been exploited to reveal information 
on the structures of proteins However, such studies require a large number (e.g., the order of one thousand) of 
homologous yet variable protein sequences.  So far, most studies have been limited to a few exemplary proteins 
for which a large number of such sequences happen to be available. Rapid advances in genome sequencing will 
soon be able to generate this many sequences for the majority of common bacterial proteins.Sequencing a large 
number of simple eukaryotes such as yeast can in principle generate similar number of common eukaryotic protein 
sequences, beyond a collection of highly amplified protein domains which already reach the necessary numbers. I 
will provide a systematic evaluation of the information contained in correlated substitution patterns for 
predicting residue contacts, a first step towards a purely sequence-based approach protein-protein interaction 
predictions, discussing some relevant subnetworks in bacteria.