Speaker
Martin Weigt
(Institute for Scientific Interchange, Torino)
Description
Experimental approaches to transient protein interactions are
laborious and serendipitous, and our understanding of
fundamental
questions like the identification of interaction surfaces or the
specificity of molecular recognition between interacting
proteins is
far from being complete. We propose a computational approach
based
on recent techniques from the statistical physics of
disordered systems,
which exploits the natural sequence variability of
homologous proteins
across hundreds of species species. Using bacterial
two-component
signal transduction (TCS) as a test case, we show that our
method is
able (i) to identify inter-protein residue contacts and to
facilitate
the prediction of protein complex strutures, and (ii) to
reconstruct a
molecular recognition code which elucidates specificity in
signal
transduction in bacteria.
