As a control, the NOXA-B peptide modelled as a monomeric α helix and gave low pAE and high pLDDT scores, confirming this as the preferred oligomerization state as expected (Fig. ,b, Fig. ). Mono_E1 was predicted to behave similarly. Modelling of the homodimeric coiled coils (CC-Di_S, CC-Di_E1 and CC-Di_E2) indicated the dimeric assemblies to be favorable, though trimers also scored favorably (Fig. ). Although multiple oligomerization states can be observed for coiled-coil sequences, previous characterization of these homodimers by analytical ultracentrifugation (AUC) confirms dimeric assemblies. The hetero-dimeric coiled coil CC-Di-A/CC-Di-B_S gave low pAE and pLDDT scores for the 1:1 peptide:protein assembly.