The hydrophobicity plot tells us about the location of transmembrane helices.
What is hydrophobicity plot?
Hydrophobicity plots are used to predict the location of turns in proteins.
In 1982, Kyte and Doolittle gave a hydrophobicity scale which gives each amino acid a hydrophobicity value.
A hydrophobicity plot is drawn between the residue number versus residue hydrophobicity.
These hydropathy plots are used to determine the transmembrane helices of proteins.
The transmembrane helices are present in the non polar area (hydrophobic) of the lipid membrane whereas the other parts are present in polar areas (hydrophilic).
Thus by computing the hydrophobicity value and plotting it on a graph we can find the loops and turns in proteins.
Nowadays there are many hydrophobicity scales determining the hydrophobicity value of amino acids.