There are many hydrophobicity scales for protein analysis.
Broadly, I gather the differences between them are from the experimental method to acquire the data and the normalisation (or lack thereof) of the data.
To detect/predict transmembrane segments one method is to use a window of 19-20 of these residue scales to detect a region of hydrophobicity above a threshold. The Eisenberg et al. scale is used by uniprot for example.
Uniprot don't seem to explain their choice of using the Eisenberg et al. scale.
Why might one use a certain scale over another when predicting transmembrane segments?