The most common method of measuring amino acid hydrophobicity is partitioning between two immiscible liquid phases. Different organic solvents are most widely used to mimic the protein interior. However, organic solvents are slightly miscible with water and the characteristics of both phases change making it difficult to obtain pure hydrophobicity scale. Nozaki and Tanford proposed the first major hydrophobicity scale for nine amino acids. Ethanol and dioxane are used as the organic solvents and the free energy of transfer of each amino acid was calculated.  Non liquid phases can also be used with partitioning methods such as micellar phases and vapor phases. Two scales have been developed using micellar phases. Fendler et al. measured the partitioning of 14 radiolabeled amino acids using sodium dodecyl sulfate (SDS) micelles. Also, amino acid side chain affinity for water was measured using vapor phases. Vapor phases represent the simplest non polar phases, because it has no interaction with the solute. The hydration potential and its correlation to the appearance of amino acids on the surface of proteins was studied by Wolfenden. Aqueous and polymer phases were used in the development of a novel partitioning scale. Partitioning methods have many drawbacks. First, it is difficult to mimic the protein interior. In addition, the role of self solvation makes using free amino acids very difficult. Moreover, hydrogen bonds that are lost in the transfer to organic solvents are not reformed but often in the interior of protein.