Extended Data Fig. 3: Trp-cage reversible folding.
Learned committor q, projected on (RMSD, dend)-space,—where the RMSD is computed with respect to basin B—from atomic coordinates of an unbiased trajectory of Trp-cage system. (A). Relative node sensitivity computed for a short unbiased simulation of 50 ns (B). Sketch of Trp-cage protein with the three main distances between atoms (green spheres) d1, d2 and d3 (C). The projection of the committor onto the (d1,d2)-subspace (D). Conformations extracted from a clustering analysis in the vicinity of the separatrix, exhibiting distinct secondary-structure elements (E, I to IV). The Trp-cage representations are colour-coded by secondary structure: white for random coils, cyan for turns, yellow for β-sheets, and magenta for α-helices.
