The knowledge of protein complex (quaternary) structure using X-ray crystallographic methods offers an atomistic glimpse into the basis of this interaction.
Therefore, structural genomics of protein complexes has been one of the frontier areas in structural biology. However, structure solution of protein complexes
must precede identification of natural/cognate binding partners in cell to allow attempt to protein co-crystallization and structure determination. The objective
of this center is to enhance methodology of identification of natural/cognate binding partners of proteins in a genomics scale. An already established ProLinks database
of genomic-context derived functional linkage information will be used to get an initial set of physically interacting candidates at 95% expected coverage. These
candidates will thereafter be screened and ranked using interaction forcefield and expectation maximization method. The sequences will be modeled to assess and
interpret the basis of the interaction as rigid bodies, and subsequently subjected to molecular dynamics simulations to confirm the viability of the protein
interaction. The candidates will be experimentally tested for protein-protein interaction screening and if successful, followed up with crystallization
and structure determination. The work is expected to give a significant boost to the structural genomics of protein complexes. The center is expected to bring forth new
ideas and lay groundwork for long term future collaborations.