(a) Sequences of PSMγ and PSMδ, highlighting tryptophan in PSMγ. (b) Helical wheel plots show sequestration of hydrophobic residues for PSMγ, PSMδ, and LL-37. Circular dichroism spectra of 20 μm PSMδ (c) or PSMγ (d) in the presence and absence of 1 mm of 2:1 POPC/POPG lipid vesicles in 20 mm potassium phosphate buffer, pH 7.3, show an α-helical structure and structural changes of PSMδ and PSMγ in the presence of lipid vesicles. Tryptophan fluorescence spectra of PSMγ in the presence and absence of 1 mm of 2:1 POPC/POPG vesicles in 20 mm potassium phosphate buffer, pH 7.3 (e), or in the presence of 5.5 M urea (f). (g) Table displaying the maximum emission wavelength of PSMγ’s tryptophan. POPC/POPG vesicles in 20 mm of potassium phosphate buffer, pH 7.3 (Kpi), cause a blue shift in the tryptophan’s maximal emission indicating an embedment of PSMγ in the lipid membrane.