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. Author manuscript; available in PMC: 2008 Jul 13.
Published in final edited form as: J Mol Biol. 2007 May 22;370(3):459–470. doi: 10.1016/j.jmb.2007.05.016

Table 1.

Amino acid sequences of the A8Q3L4 family of peptides used in this study, including computed hydrophobic moments and partitioning free energies.

Amino Acid Sequence Name Hydrophobic a moment (μH) bΔGWW (kcal mol−1)
AC-LQALAAQALQAAALA-GW-NH2 A8Q3L4-0.55 0.55 −3.53
Ac-LAQAAALQLLAAQAA-GW-NH2 A8Q3L4-2.00 2.00 −3.53
Ac-AQLAALAALQAAQLA-GW-NH2 A8Q3L4-2.86 2.86 −3.53
Ac-AAAQAAAQLLQALLA-GW-NH2 A8Q3L4-4.72 4.72 −3.53
Ac-QLAQALAAALAALAQ-GW-NH2 A8Q3L4-5.51 5.51 −3.53
Ac-QALQALAAALAALAQ-GW-NH2 A8Q3L4-5.54 5.54 −3.53
a

Hydrophobic moments were computed using the Totalizer module of MPEx, available over the World Wide Web: http://blanco.biomol.uci.edu/mpex

b

Free energies of transfer from water to bilayer interface based upon the Wimley-White17 experiment-based interfacial hydrophobicity scale. These were also computed using the Totalizer module of MPEx (above).