The hydrophobic effect is a crucial driver for many biomolecular interactions, including protein folding, protein-protein association, protein-ligand binding, and micelle formation. Among these, protein-protein interactions are significant for most physiological and pathological processes, such as immune response, signal transduction, and enzyme catalysis. The protein-protein interaction interfaces involve hydrophobic patches, which are not only influenced by the chemistry of the underlying amino acid residues but also depend on the surface patterns. The previously reported approaches either fail to capture the chemical and geometrical patterns of the heterogeneous surface or are computationally expensive. We have developed a new computational method that provides the collective response of water to the topological features of the proteins. We investigated an array of globular and intrinsically disordered proteins and identified hydrophobic patches of proteins that lead to protein assembly. The results are in excellent agreement with those published in the literature. Our results show that amino acids exhibit disparate hydration properties depending on the local topography of the protein. In addition, this method enables us to quantitatively compare the hydrophobicity of different proteins relative to each other.