In the study of lipid systems, biological solid-state NMR has historically concentrated on characterization of relatively simple model membranes. In more recent times, peptides and proteins that interact with these membrane systems have increasingly shared the focus. Here we describe how solid-state NMR provides information about the effect of antimicrobial peptides (AMPs) on membrane bilayers, and their location relative to the membrane surface, and their structure in the context of the membrane. Aligned membrane bilayers and bicelles, and magic angle spinning techniques using unoriented bilayers are discussed, together with measurements of chemical shift anisotropy and dipolar couplings to gain structural details of AMPs in membranes. In addition to 31P, 2H and 14N NMR of phospholipid bilayers, 19F, 13C and 15N NMR of labelled AMP, gramicidin A′, magainin 2, PGLa, aurein 1.2 and protegrin-1, are reviewed.
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