For both CC-Tri_E1 and CC-Tet_E1, monomeric, trimeric and tetrameric assemblies were predicted to be accessible (Fig. ). The targeted oligomer states all aligned well with crystal structures of the parent coiled-coil oligomers (Fig. ). Next, to give insight on preferred scaffold/protein stoichiometries, models were generated for scaffolds in their designed oligomerization state (i.e. a coiled-coil dimer for dimeric sequences, a coiled-coil trimer for the trimeric sequence, etc.) bound to one through n copies of the MCL-1 protein (where n is the expected oligomerization state of the peptide) (examples in Fig. ).