Besides the force field parameters, the number of SDS molecules per micelle has to be set manually in molecular dynamics simulations, because simulations of spontaneous aggregation in large systems are not feasible at atomistic resolution. For preliminary screening, we simulated each peptide in a micelle with the sizes of 40, 45 and 50 SDS molecules for about 300 ns. In this quick scan, systems with 50 SDS molecules reproduced the experimental spin relaxation data quite well for all the peptides except GWALP. Due to the substantial computational cost, we performed a more systematic study on the micelle size dependence only for hMff(TA) which indicated the strongest size dependence in the initial screening. For this, we simulated hMff(TA) in micelles with 40, 45, 50, and 60 SDS molecules. Each system was simulated for at least 3 µs and repeated 3 times from different initial configurations.