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. 2003 Dec;85(6):3769–3780. doi: 10.1016/S0006-3495(03)74792-4

FIGURE 2.

FIGURE 2

Hydrophobic moments (as a function of the δ angle) calculated according to different hydropathy scales. (A) Comparison using WW hydrophobicity-at-interface (left panel) or Eisenberg hydrophobicity (right panel). The selected sequences WWEEWEEWWEEWEE (solid lines) and IIRRIRRIIRRIRR (dotted lines) contain, alternating with helical periodicity, most hydrophobic and most hydrophilic residues in WW and Eisenberg scales, respectively. (B) Hydrophobic moment of the HIV-1 gp160 664–674 segment (∼3 helical turns) calculated as a function of the δ angle. Sequences derived from wild-type (solid lines) and W(1–3)A mutant (dotted lines) proteins are compared using three different hydrophobicity scales (WW, Eisenberg, and KD). Dashed line in WW panel corresponds to the 673–683 gp160 stretch.