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. Author manuscript; available in PMC: 2009 Nov 1.
Published in final edited form as: Biochim Biophys Acta. 2008 Jul 25;1778(11):2544–2554. doi: 10.1016/j.bbamem.2008.07.013

Figure 12.

Figure 12

Models of SP-B59-80 interactions with the two lipid environments studied assuming a helical peptide conformation. (Left) Based on 2H NMR data, SP-B59-80 deeply penetrates into 4:1 DPPC:POPG lipid bilayers. (Right) In contrast, in 3:1 POPC:POPG MLVs lipids, a more peripheral interaction of SP-B59-80 with the lipid headgroup region is proposed. A transmembrane orientation of the peptide is unlikely as it would place four polar residues in the hydrophobic interior.