The hyperactivity of RAS proteins is associated with tumor progression, invasion, and metastasis in many forms of cancer. RAS proteins must directly interact with the membrane to activate their signaling targets, but the complexity and dynamics of such interactions continue to defy experimental characterization. In a multi-institute collaboration, combining NMR with multi-μs MD simulations with NAMD, and neutron reflectometry, we developed for the first time how a membrane-binding protein domain interacts with and penetrates the surface of the cell at full atomic detail. Analysis of the simulations in VMD revealed that the protein adopts multiple forms on the membrane in a lipid-dependent manner. More details can be found in a recent publication in Nature Communications.