Most of the existing hydrophobicity scales are derived from the properties of amino acids in their free forms or as a part of a short peptide. Bandyopadhyay-Mehler hydrophobicity scale was based on partitioning of amino acids in the context of protein structure. Protein structure is a complex mosaic of various dielectric medium generated by arrangement of different amino acids. Hence, different parts of the protein structure most likely would  behave as solvents with different dielectric values. For simplicity, each protein structure was considered as an immiscible mixture of two solvents, protein interior and protein exterior. The local environment around individual amino acid  (termed as "micro-environment") was computed for both protein interior and protein exterior. The ratio gives the relative hydrophobicity scale for individual amino acids. Computation was trained on high resolution protein crystal structures. This quantitative descriptor for microenvironment was derived from the octanol-water partition coefficient, (known as Rekker's Fragmental Constants) widely used for pharmacophores. This scale well correlate with the existing methods, based on partitioning and free energy computations. Advantage of this scale is it is more realistic, as it is in the context of real protein structures.