To further investigate the stability of transmembrane dimers in Martini 3 and to test OLIVES on proteins with diverse secondary structure content, we chose an E. coli homolog of the ClC chloride channel family as our final test system. The fold of ClC chloride channel consists of an exclusively α-helical bundle with two structurally similar transmembrane domains exhibiting pseudo two-fold symmetry. The monomer fold is predominantly stabilized by hydrophobic contacts and out of the 441 residues in native contacts, 318 are hydrophobic (SI Figure ). Compared to the OMPLA protein with β-sheet secondary structure with a polar interior stabilized by hydrogen bond networks, the ClC channel represents a distinct end of the spectrum with a complete α-helix secondary structure content stabilized by mainly hydrophobic interactions. The ClC chloride channel forms a functional homodimer (Figure ,A) which has been extensively studied both experimentally and computationally by Chadda et al. The dimer interface consists of 8 short helices (4 on each monomer) which contribute to a significant hydrophobic mismatch to the bilayer in the monomer state, thought to drive dimerization. The interface native contacts are also of hydrophobic character with 77 out of 137 residues in contacts being hydrophobic (SI Figure ).