Nanometer-scale order, compartmentalization, and heterogeneity make lipid membranes significantly richer in complexity compared to previous models (Figure , right). Modern models incorporate compositions containing a huge diversity of components, as observed in modern lipidomic analyses . One key aspect of modern lipid membrane models is the presence of compartmentalized domains with distinct lipid and protein compositions, referred to as "lipid rafts" that have been observed in artificial and biological membranes. There are clear implications to biological functions that result from colocalizing proteins, as well as modulating the local environment around certain proteins . Rafts have remained a topic of discussion for over a decade, and this stems mainly from the difficulty in experimentally characterizing their nanometerscale structure and composition with current techniques. In addition, the concept of rafts rests on the idea of stable domains enriched in certain lipids. Experiments and simulations currently support a more nuanced picture than the lipid raft model, suggesting the formation of dynamic multicomponent local environments that results in transient interactions with specific lipid species, termed the "functional paralipidome" . While transient changes in local membrane composition can influence the protein conformational landscape, the molecular mechanisms connecting environments with protein modulation are not understood. While techniques such as cryo-EM have revolutionized the field of membrane structural biology, measuring lipid heterogeneity remains extremely difficult, due to a lack of techniques that provide species-specific local environments. Beyond structural measures, there is virtually no time-resolved measurement that can serve to understand the coupling between protein and lipid dynamics across timescales .