Furthermore, we used our approach to understand indirect relations between peptide backbone N spin relaxation times and conformational ensembles. We found significant correlations of helical propensities of peptide residues with large hetNOE and low T 2 values, particularly when compared with the other residues within the same peptide. On the other hand, T 1 values mainly correlated with the overall rotation of peptides. These relations enable rapid interpretations of peptide conformations in detergent aggregates from spin relaxation times even when MD simulation data is not available.