Cabezudo and co-workers assign the erroneous behavior of Martini 3 to excessively strong peptide-water interactions , which parallels the excessive-hydrophilicity hypothesis we put forth above for the lack of aggregation of coiled coil dimers. Indeed, excessive protein-water interactions would selectively stabilize the water-exposed adsorbed state. They would also lower the TM-to-adsorbed energy barrier: as a peptide's end dives across the membrane core, it progressively allows residues on the opposite end to come into contact with increasing amounts of water; the water interactions of those residues, if too strong, then overly compensate the cost of moving the diving end's polar moieties through the core. Such a lowering of this energy barrier is likely the reason why we were able to observe TM peptide ejection in the µs scale.