The negatively-charged membrane, then the hydrophobic side-chains insert between the lipid acyl-chains, and
finally the helix folds in order to contain hydrophilic residues and lower its energy (Drin and Antonny, 2010). Hence the hydrophobic patch (Fig. 2A, 5B, yellow residues) of the MurG 18 amino acid amphipathic helix is probably embedded within the lipid aliphatic chains of the