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. Author manuscript; available in PMC: 2015 Nov 1.
Published in final edited form as: Arch Toxicol. 2014 Sep 12;88(11):1965–1985. doi: 10.1007/s00204-014-1357-9

Fig. 3.

Fig. 3

Single-molecule FRET investigation of the hammerhead ribozyme. a Full-length hammerhead ribozyme used in the studies discussed. The labeling sites for single-mol ecule FRET are indicated at the top, and the mutations used to disrupt loop-loop interactions are shown in the bottom-left. b Single-molecule FRET histograms showing the effect of magnesium concentration and loop mutations on the conformations adopted by wild-type (left panel) and two mutant (center and right panels) ribozymes. The active, high-FRET conformation is sampled only by the wild-type ribozyme, and only under high magnesium conditions (McDowell et al. 2010)