TABLE 1.

Hydrophobic moment 〈μ〉 and polar angle Φ of KLAL, l₁₁k₁₂-KLAL and k₉a₁₀-KLAL calculated for an α-helical and a β-sheet secondary structure with different hydrophobicity scales

Peptide		〈μ〉 (consensus)	〈μ〉 (OMH)	〈μ〉 (WRH)	Φ
KLAL	α-helix	0.334	0.120	0.377	80
	β-sheet	0.328	0.543	0.600
l11k12-KLAL	α-helix	0.267	0.060	0.254	160
	β-sheet	0.214	0.419	0.422
k9a10-KLAL	α-helix	0.296	0.105	0.375	75
	β-sheet	0.381	0.545	0.645

The angle ω between the amino acid side chains for the α-helix and the β-sheet structure was fixed at 100° and 167°, respectively. The mean hydrophobicity per residue, H, according to the different hydrophobicity scales of the peptides is −0.016 (consensus), 0.147 (OMH), and −0.344 (WRH).