where k B is a Boltzmann constant, T is the temperature, η is the viscosity of water, r is the radius, D r is the rotational diffusion coefficient, and τ is the timescale of the rotational dynamics of a rigid spherical object. The radii of micelles were approximated using the radius of gyration. Because not all SDS molecules remain within a micelle throughout the simulation in some systems, we first determined which molecules are part of the micelle in simulations separately for each time step. This was done by selecting SDS molecules with any atom closer to any peptide atom than a cut-off distance of 1.4-1.8 nm. The cut-off distance was set system specifically to give the most reasonable results as exemplified for eYqjD(TA) simulation with 50 SDS molecules in figure where cut-off value 1.8 nm was used. The radii of gyrations were then calculated using these molecules together with the peptide(s) first separately for each configuration and then averaged over time. The number of SDS molecules in a micelle as a function of time was also used to monitor the equilibration of simulations as exemplified in figure . The average number of SDS molecules within a micelle in each simulation is reported in Tables and. These analyses were performed with Python scripts utilizing the MDAnalysis package. Propensities of secondary structures in peptides were calculated using DSSP plug-in in Gromacs. The propensity of individual secondary structural motives was averaged over the time of trajectories. The local environment helicity propensity of a residue was correlated with the T 1 , T 2 and hetNOE value of the residue for all peptides and simulations.