All the peptides used in this work are alpha-helical. Their Martini 2.2 and Martini 3 CG topologies were created from atomistic structures (see Table for sequences) using the mar-tinize2 script. For the coiled coil systems, the GCN4leucine zipper mutant N16K parallel homodimer (PDB id: 1ZIK) and the IAAL-E3/K3 synthetic parallel heterodimer (PDB id: 1U0I, model 1/20) were used as starting points; Martini 2 and 3 topologies were generated using angle/torsion restraints to enforce helicity, and for Martini 3 additional topologies were created with elastic restraint networks, using mar-tinize2's default parameters. For the TM WALPs, ideal αhelical structures were created from their sequence using the Avogadro software and the Martini 2/3 topologies constructed using only angle/torsion secondary structure restraints. WALPs are capped on both termini, with N-terminal acetylation and C-terminal n-methyl amidation (Table ); since neither capping group has been explicitly parameterized for Martini, we modeled them by simply assigning a non-charged, randomcoil, backbone particle type to the WALP's terminal beads (type P5 in Martini 2 and P2 in Martini 3).