Another potential cause for WALP16's TM-to-adsorbed ejection could be the way we modeled the peptides' termini. Since neither Martini model has parameters for the WALPs' Nterminal acetylations or C-terminal n-methyl amidations, we simply considered each terminal bead to be uncharged, and did not add any extra particles. As a consequence, WALPs are marginally shorter than if termini caps had been explicitly modeled, which could have exacerbated the negative size mismatch of WALP16 beyond the point of TM stability. However, we were able to observe the same instability behavior, at a larger timescale, for one of the WALP19 replicates (see Figure ). If the shortening of termini caps were indeed the destabilizing aspect for WALP16, then WALP19, with 3 extra residues, should have remained transmembranar.