Fig. 2.

The first contact time (black circles connected by black lines) and stabilization time (red circles connected by red lines) vs. the distances between C^αs of selected pairs of residues of hairpin 1 (D1 → Ala14 and Gly16, D2 → Thr13 and Lys17, D3 → Lys12 and Thr18, D4 → Tyr11 and Tyr19, D5 → Glu10 and Tyr20, D6 → Thr9 and Tyr21, and D7 → Trp8 and Asn22) and hairpin 2 (D8 → Asn23 and Asp26, D9 → Asn22 and Glu27, D10 → Tyr21 and Ser28, D11 → Tyr20 and Thr29, and D12 → Tyr19 and Trp30) and also, vs. the distances between C^αs (C^βs are represented by white circles connected by dashed lines) of only nonpolar residues of hairpin 1 (D1 → Ala14 and Gly16, D2 → Tyr11 and Tyr19, and D3 → Trp8 and Tyr20) and hairpin 2 (D5 → Tyr20 and Pro33 and D6 → Tyr19 and Trp30) for (A and B) three-state, (C and D) two-state, and (E and F) downhill folding trajectories of the L26D mutant and (G and H) the downhill folding trajectory of the L26W mutant (D8 → Asn23 and Trp26 in G and D4 → Tyr21 and Trp26 in H). Structure of L26D is illustrated in I. Horizontal green dashed lines indicate the folding time of L26D and L26W.