Fig. 1.

MD simulations of the three λ_6–85 multiprobe mutants. (A) Time trajectories of Q and rmsd based on α-carbon atoms of the λ_6–85 crystallographic state [PDB ID code 3KZ3 (33)]. Red dashed vertical lines indicate the time points when the proteins visited the folded state. (B) Simulation protocol (details are provided in SI Appendix, section 2 and Table S1). The unfolded WT from our previous study (18) was mutated and simulated at 5,000 bar and 340 or 350 K before jumping the pressure down to 1 bar. (C) Close-up view of time dynamics of Q (orange) and rmsd (black) near the folded states. Horizontal lines correspond to Q_max = 0.8 (orange) and rmsd = 2.5 Å (black). The crystallographic state (gray) overlapped with the simulated structures of each mutant at the time when these mutants visited the folded state with Q_max = ∼0.8 (21.0 μs for λ₁₂, 15.0 μs for λ₃₂, and 51.5 μs for λ₁₃). Distances between residues used in fluorescence measurements are shown with colored lines (contact 1–2 in blue, contact 3–2 in green, and contact 1–3 in red).