Structure and dynamics of the lipid modifications of a transmembrane α-helical peptide determined by 2H solid-state NMR spectroscopy

► Transmembrane α-helical peptides with lipid chains attached were investigated. ► Lipid chains with 8 or more carbons fully insert into the membrane. ► No chain matching of those chains with the length of the host membrane was observed. ► Chains could exert a stabilizing effect on the peptide.