To experimentally characterize the dynamics of the selected six peptides in SDS micelle systems, we measured T 1 , T 2 , and hetNOE spin relaxation times of N atoms that were specifically labelled in peptide backbone in positions shown in Fig. a. All the labelled residues were visible in HSQC spectra with the exception of labelled N-terminal residues of hMff(TA) and yFis1(TA). HSQC spectra with the assignments and resulting spin relaxation times are shown in Figs and, respectively. For T 1 spin relaxation time, we observe an increasing trend in the order of eElaB(TA) < eYqjD(TA) < Magainin 2 < hMff(TA) < yFis1(TA) < GWALP, while the trend in T 2 is exactly opposite. Mitochondria-directed tail anchor proteins, eElaB(TA) and eYqjD(TA) derived from E. coli proteins have lower T 1 values and higher T 2 values than hMff(TA) and yFis1(TA) from humans and yeast. For peripheral Magainin 2 peptide, T 1 and T 2 times lay between values for tail anchors, while transmembrane GWALP has higher T 1 and lower T 2 values than any other peptide. HetNOE values lie between 0.4-1.0 for all the studied peptides, and systematic differences between peptides are not observed. ns range in magnetic field dependent manner. However, the interpretation of molecular dynamics from spin relaxation times is not straightforward, particularly for peptides in micelles where the detergent environment affects peptide dynamics in a non-trivial manner and standard models for protein dynamics may not be valid. Therefore, we rely here on interpretation from MD simulation models with detergents explicitly included in the following sections.