To gauge the role of the aromatic residues W238 and F241 in maintaining a stable binding pose, an alanine double mutant (W238A241A) was designed and simulated across 5 replicas for 1 µs simulation time. Simulations were run from the same initial state as substrate-protein simulations. In these simulations, h-cisPT does not dissociate from the membrane (Fig. ), though the residues in the neighborhood of 235-245 no longer makes consistent membrane contact. However, contact analysis of these simulations (Figure ) shows that the reduction in membrane-protein contacts is greater than the amount of contacts made by the 235 to 245 region in wild type proteins. This indicates that, while the h-cisPT does not dissociate from the membrane, regions outside the modified helix are also making reduced contact with the membrane. Qualitative observation of simulated trajectories suggested that the mutant protein was unable to maintain a stable binding pose, rotating and swaying around the membrane-associated n-terminal. To quantify this change in stability of pose, we measure the distribution of the angle between the membrane normal axis and the vector connecting N-terminus and residues 15 and 241. If the angle is 0°the vector and the membrane normal axis are co-linear, while if the angle is 90°the vector connecting these key membrane binding residues would be orthogonal to the membrane normal, and implies that the 20