  Understanding how a stressor applied on a biological system shapes its
evolution is key to achieving targeted evolutionary control. Here we present a
toy model of two interacting lattice proteins to quantify the response to the
selective pressure defined by the binding energy. We generate sequence data of
proteins and study how the sequence and structural properties of dimers are
affected by the applied selective pressure, both during the evolutionary
process and in the stationary regime. In particular we show that internal
contacts of native structures lose strength, while inter-structure contacts are
strengthened due to the folding-binding competition. We discuss how
dimerization is achieved through enhanced mutability on the interacting faces,
and how the designability of each native structure changes upon introduction of
the stressor.
