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. 2004 May 17;32(9):2707–2715. doi: 10.1093/nar/gkh588

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Interactions of the Fl/TMR junction with aminoglycosides. (A) The Fl/TMR 3WJ (20 nM, black) was titrated with gentamicin (red), hygromycin (green), kanamycin (blue), neomycin (cyan), paromomycin (magenta), streptomycin (dark yellow) and tobramycin (brown). The ratio of Fl/TMR emission is monitored as a probe for junction folding. (B) Titration of the Fl/TMR 3WJ (20 nM, black) with S15-TR in the presence of 5 mM aminoglycoside. The color scheme is the same as in (A). The ratio of TMR/TR emission is monitored as a probe for S15 binding. While all aminoglycosides appear to stabilize the folded conformer of the junction with different concentration dependence, none of them inhibits S15 binding.

Interactions of the Fl/TMR junction with aminoglycosides. (A) The Fl/TMR 3WJ (20 nM, black) was titrated with gentamicin (red), hygromycin (green), kanamycin (blue), neomycin (cyan), paromomycin (magenta), streptomycin (dark yellow) and tobramycin (brown). The ratio of Fl/TMR emission is monitored as a probe for junction folding. (B) Titration of the Fl/TMR 3WJ (20 nM, black) with S15-TR in the presence of 5 mM aminoglycoside. The color scheme is the same as in (A). The ratio of TMR/TR emission is monitored as a probe for S15 binding. While all aminoglycosides appear to stabilize the folded conformer of the junction with different concentration dependence, none of them inhibits S15 binding.