  The influence of the patchiness and correlations in the distribution of
hydrophobic and polar residues at the interface between two rigid biomolecules
on their recognition ability is investigated in idealised coarse-grained
lattice models. A general two-stage approach is utilised where an ensemble of
probe molecules is designed first and the recognition ability of the probe
ensemble is related to the free energy of association with both the target
molecule and a different rival molecule in a second step. The influence of
correlation effects are investigated using numerical Monte Carlo techniques and
mean field methods. Correlations lead to different optimum characteristic
lengths of the hydrophobic and polar patches for the mutual design of the two
biomolecules on the one hand and their recognition ability in the presence of
other molecules on the other hand.
