Abstract

In nature, there are proteins or protein complexes that are pseudo-symmetrical, as they consist of domains or subunits that are similar but not identical to each other. It is likely that they started out as fully symmetrical, but then over the course of evolution changed to become asymmetrical in adaptation to new functions Thus, amino acid residue relevant to those new functions can be identified by analysing the pseudo-symmetry of these proteins and protein complexes. In this project, we will develop a new scoring method for pseudo-symmetry and apply it to protein families with two-fold, three-fold and inverted topologies to identify amino acid residues that are key to the function of these proteins using sequence information alone. The project is well-defined.