Our recent solid-state NMR and EPR studies have identified differences in the lipid binding behaviour of wild-type and mutant puroindoline B proteins. These studies have shown changes in lipid headgroup dynamics which occur on binding of these proteins to model anionic membranes, and suggest differences in the depth of membrane penetration that are likely to impact on the potential mode of action of the proteins in vivo. The availability of non-racemic POPG-(2H)2 presents an opportunity to characterise protein binding to the lipid head group region by neutron reflectivity. In this continuation proposal we request beamtime to complete studies at a temperature above the lipid phase transition temperature in order to probe behaviour in the liquid phase.