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. Author manuscript; available in PMC: 2016 Feb 16.
Published in final edited form as: Biochemistry. 2016 Feb 3;55(6):837–849. doi: 10.1021/acs.biochem.5b00965

Table 1.

Binding affinities of analogs measured for the ydaO riboswitch

Modification Analog Kd (nM) Fold Loss ΔΔGbind (kcal/mol)
c-di-AMP 0.43 ± 0.02
Base c-AMP-GMP > 2.3 × 106a > 4.2 × 106 > 9.0
c-di-GMP > 1.1 × 107 > 2.0 × 107 > 10
c-AMP-IMP 750 ± 43 1400 4.3
c-di-IMP 2000 ± 460 3600 4.9
c-AMP-Purine 18 ± 1.6 33 2.1
c-di-Purine 2900 ± 270 5300 5.1
c-di-N6m,N6mAMP > 5 × 105 > 9.1 × 105 > 8.1
c-AMP-DAP 360 ± 38 650 3.8
c-di-DAP > 1.5 × 106 > 2.7 × 106 > 8.8
c-di-2AP > 2.5 × 106 > 4.5 × 106 > 9.1
c-di-c7AMP 6.4 ± 0.6 12 1.5
Ribose c-dA-AMP 11 ± 1.6 20 1.8
c-di-dAMP 160 ± 13 290 3.4
c-2’F-A-AMP 26 ± 2.4 47 2.3
c-di-2’F-AMP 2800 ± 330 5100 5.1
c-dA-2’F-A 290 ± 23 530 3.7
c-2’OMe-A-AMP 340 ± 41 620 3.8
c-di-2’OMe-AMP > 1.6 × 106 > 2.9 × 106 > 8.8
Phosphate c-(RpRp)-di-Aps 1.0 ± 0.1 1.8 0.4
c-(RpSp)-di-Aps 1.6 ± 0.4 2.9 0.6
a

No detectable binding at the highest ligand concentration tested (≥200 µM). Kd values were estimated based on a 5% detection limit.