Dynamic interactions of peptides with membranes and other lipid aggregates are crucial in many biological functions and biomedical applications. For example, fusion peptides play an important role in virus entry into host cells, antimicrobial peptides can be used as therapeutical agents, signal peptides regulate protein translocation in cells, and apolipoprotein mimetic peptides stabilize nanodiscs with potential pharmaceutical and other applications. However, peptides are small and their dynamic interactions with membranes are difficult to capture by most experimental methods that access atomistic resolution data of biomolecular systems, such as crystallography or electron microscopy. Nuclear magnetic resonance (NMR) experiments are sensitive to fast (ps to µs) timescale motions of small molecules, but their applications are often limited by complications in sample preparation and in interpretation of the data.