Starting configurations for simulations with two GWALP, yFis1(TA), or eElaB(TA) pep-tides within the same micelle were prepared by (i) removing water molecules from an equilibrated snapshot of a monomeric system, (ii) adding a second peptide to close proximity of the micelle, (iii) solvating the system again. For the GWALP peptide, such simulations were run with 40, 45, 50, and 60 SDS molecules. In the simulation with 50 SDS molecules, two GWALP peptides started to interact with each other and created a dimer where the two peptides rotated together in the micelle, see Figure ). Therefore, with the optimal micelle size of 70 SDS, we ran replicas starting from conformations with (together) and without (separate) mutual interactions of two GWALP peptides. In all of the "together" simulations, peptides stayed in the form of the dimer for the whole length of the simulations. One of the systems with a "separate" starting configuration indicated potential dimer formation at the end of the simulation, while peptides retained independent motions otherwise. Simulations with systems having two peptides in the same micelle are summarized in Table .