At least one appears to be amphipathic with hydrophobic and hydrophilic residues on opposite faces.

Long stretches of hydrophobic residues may indicate transmembrane helices.

These hydrophobic residues might mediate the interaction with the target proteins and therefore receptor recognition.

To this end, a thermostable protease is used, which cleaves specifically at exposed hydrophobic residues.

Both the second and fourth scales place cysteine as the most hydrophobic residue, unlike the other two scales.

CP is a 120 amino acid protein, containing 40% hydrophobic residues.

The outer surface of the β sheet also has many conserved hydrophobic and basic residues.

Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin.

Among the hydrophobic residues, aromatic amino-acids are found to have the highest amyloidogenic propensity.

The interior of the domain contains additional small clusters of glycines, but few other hydrophobic residues.