The full dynamic landscapes for proteins with all observed timescales and their weights are shown in Fig. in the supplementary information, while a more comprehensible pre-sentation where the weight of each timescale is represented by the point size is shown in Because the differences in dominant timescales between peptides correlate with the differences in T 1 times, we conclude that the experimentally observed differences in T 1 values arise from differences in overall rotational dynamics between peptides. In conclusion, our results indicate a dynamic conception of peptide-micelle complexes where the rotation of peptides is dominated by nanosecond timescale dynamics related to their overall motion that can be experimentally detected by T 1 values. Because peptides rotate independently from detergents in a viscous media formed by the micelle, the rotation of the peptide-micelle complex cannot be described by the Stokes-Einstein equation that assumes that peptides and detergents rotate together as a spherical rigid body.