Recognition of protein complexation based on hydrophobicity distribution

The identification of the surface area able to generate the protein-protein complexation ligand and ion ligation is critical for the recognitionof the biological function of particular proteins. The technique based on the analysis of the irregularity of hydrophobicity distribution is usedas the criterion for the recognition of the interaction regions. Particularly, the exposure of hydrophobic residues on the surface of protein aswell as the localization of the hydrophilic residues in the hydrophobic core is treated as potential area ready to interact with externalmolecules. The model based on the “fuzzy oil drop” approach treating the protein molecule as the drop of hydrophobicity concentrated inthe central part of structure with the hydrophobicity close to zero on the surface according to 3-dimensional Gauss function. The comparisonwith the observed hydrophobicy in particular protein reveals some irregularities. These irregularities seem to represent the aim-orientedlocalization.