
Magnesium stabilizes the low FRET conformation. (A) Typical FRET trajectories of the unmodified U2–U6 complex in 10 mM (top) and 40 mM Mg2+ (bottom). (B) FRET histograms of the unmodified U2–U6 complex obtained in 10 mM (top) and 40 mM Mg2+ (bottom). Both FRET trajectories and histograms exhibit three FRET states: low FRET (∼0.2, G), mid FRET (∼0.4, I), and high FRET (∼0.6, N). (C) Observed folding rate constants (k1, k−1, k2, and k−2) of the hU2–U6 complex without post-transcriptionally modified bases in 10 mM (red) and 40 mM Mg2+ (purple). (D) Effect of Mg2+ on the folding energy landscape of the hU2–U6 complex.










