Furthermore, we investigated whether dimerization could explain distinct spin relaxation times for GWALP by simulating two peptides in micelles with different numbers of SDS molecules. Results in Fig. show that we can reproduce the experimental T 1 spin relaxation data either with one GWALP peptide in a micelle with 80 SDS molecules or with two GWALP peptides in a micelle with 70 SDS molecules. For systems with two GWALP peptides in an SDS micelle, we observe two different scenarios: peptides either strongly interact with each other, creating a dimer that rotates in the micelle as one entity, or the two peptides continue to rotate independently, see Figs. S1 a) and b) in the supplementary information. We observe slight differences between these two scenarios in terms of T 1 spin relaxation times. Magainin 2 < hMff(TA) yFis1(TA) < GWALP. Notably, after selecting the force field parameters and the number of molecules in the simulation system, no further fitting is made to reproduce the experimental data. Therefore, the selected simulations predict experimental spin relaxation times directly from physical interactions between atoms with relatively good accuracy, which justifies their further usage in interpreting the dynamic landscape of peptides in micellar environments performed in the next sections.