The Wimley–White whole residue hydrophobicity scales are significant for two reasons. First, they include the contributions of the peptide bonds as well as the sidechains, providing absolute values. Second, they are based on direct, experimentally determined values for transfer free energies of polypeptides.
Two whole-residue hydrophobicity scales have been measured:
* One for the transfer of unfolded chains from water to the bilayer interface (referred to as the Wimley–White interfacial hydrophobicity scale).
* One for the transfer of unfolded chains into octanol, which is relevant to the hydrocarbon core of a bilayer.
The Stephen H. White website provides an example of whole residue hydrophobicity scales showing the free energy of transfer ΔG(kcal/mol) from water to POPC  interface and to n-octanol. These two scales are then used together to make Whole residue hydropathy plots. The hydropathy plot constructed using ΔG − ΔG shows favorable peaks on the absolute scale that correspond to the known TM helices. Thus, the whole residue hydropathy plots illustrate why transmembrane segments prefer a transmembrane location rather than a surface one.