where F (R ij ) and f (r ij ) are two sigmoid functions. The form of these functions ensures that points lying close together in the high-dimensional space, which most likely belong to the same conformational basin, are then projected close together. Points that are far apart, and are thus likely to be in basins that are not connected by a single transition state, are projected far apart. For our analysis, the high-dimensionality data set consisted of the 20 backbone dihedrals of the peptide, excluding the terminal residues. The σ of both sigmoids was set at 5.5 and the a and b parameters were chosen as 12 and 7, and 1 and 2, for the high (20D) and low (2D) dimensionality functions, respectively. The resulting maps were colored with respect to: the GROMOS clustering, the radius of gyration, and the left-handed polyproline II helix (PPII) secondary-structure content. The latter was computed using the ALPHABETA collective variable implemented in PLUMED, that measures a distance between the instantaneous values of a set of torsional angles and set of reference values.