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Hydropathy plots show the hydrophobic nature of polypeptide regions. They can be used to locate α helical transmembrane segments in a polypeptide. Identify which segment(s) of the polypeptide characterized in the hydropathy plot below could belong to a transmembrane region of a protein.
Positive values indicate hydrophobic regions; negative values indicate hydrophilic regions. Hydrophobic amino acid residues are more likely to be found within a membrane. Hydrophilic residues are more likely to be exposed to the solvent and on the surface of a protein. Typically, membrane-spanning regions have values above 1.6. Your answer would have to lie above zero

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Positive values indicate hydrophobic regions; negative values indicate hydrophilic regions.

Using hydropathy charts, one can see how hydrophobicity changes over the course of a peptide sequence. The 20 amino acids' hydrophobic and hydrophilic characteristics are used to create a hydropathy scale. Each point in the sequence's total hydropathy is determined by a shifting "window" (Y coordinate). After that, these amounts are plotted against the corresponding places (X coordinate). Such plots are helpful in identifying the membrane-spanning sections of membrane-bound proteins as well as the hydrophobic interior regions of globular proteins.

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