To demonstrate the practical advances of our approach, we determined the dynamic landscape of peptide-detergent aggregates for the first time. Our findings support a view of peptide dynamics within a detergent matrix in which peptides and detergent molecules do not rotate together as a rigid body in solvent. Rather, peptides rotate in a viscous medium composed of detergent micelle. Based on our interpretation of peptide backbone 15 N spin relaxation times, the rotation of analyzed peptides in detergent aggregates was dominated by timescales between approximately 4-8 ns which we interpret to arise from the overall rotation of peptides. We explain the substantially slower overall rotation observed for transmembrane GWALP peptide, with the timescale of ∼8 ns, by its preference for larger detergent aggregates than peripheral Magainin 2 or mitochondria tail anchor peptides having overall rotational timescales of ∼4-6 ns. This result supports previous studies suggesting that mitochondria tail anchor peptides are more similar to peripheral peptides than transmembrane peptides. On the other hand, the rotational dynamics of SDS molecules forming the detergents is dominated by timescales faster than 100 ps while ns timescales dominating in embedded peptides are absent.