Table S4.

Simulations and helix formation during simulation

Research group	Method	protein	TSE, when possible	Folding pathway
Shoemaker et al. (15)	Go-like, 1 bead per residue	λWT	α1–α4	(α1–α4) ⇒ +α5
Allen et al.(16)	Go-like, 1 bead per residue	λWT	All helices present in DSE at 70+%	(α1–α4) ⇒ +α5 or (α1, α2, α4) ⇒ +α3 ⇒ +α5
Pogorelov and Luthey-Schulten (62)	All-atom MD (CHARMM) with Go-like potential	λWT		(α1, α2, α4) ⇒ +α5 ⇒ +α3
		λYA		(α1, α2, α4) ⇒ +α3 ⇒ +α5
Adhikari et al. (13, 14)	TerItFix (MCSA), Cβ level chain	λD14A	α1, α3, α4	(α1, α3, α4) ⇒ +α2 ⇒ +α5
Bowman et al. (18)	MSM with all-atom MD (AMBER03)	λD14A	P1/2 and later structures have variable β and α content†	(α1, α4) ⇒ +(α2, α3) ⇒ α5
Lindorff-Larsen et al. (19)	All-atom MD (CHARMM22*)	λD14A	TSE contains 94% secondary structure and α5 less than α1–α4	(α1, α4) ⇒ +(α2, α3) ⇒ α5 or (α1–α4) ⇒ +α5‡
Liu et al. (17)	All-atom MD (CHARMM22+CMAP)	λHG		(α1–α3) ⇒ +(α4, α5)

^†Simulations that avoid starting from beta conformers fold more directly to the native state on a faster timescale (18).

^‡Using transition path analysis of 14 folding and 16 unfolding transition pathways (36).