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. Author manuscript; available in PMC: 2008 Dec 8.
Published in final edited form as: Biochemistry. 2007 Mar 27;46(16):4861–4875. doi: 10.1021/bi062169g

Table 4.

Binding of the +1 U•U Mismatched Substrate

CCUCdT- Δ ΔGbp (kcal/mol)
kc (min−1) Ktert
−G +G
-AAACC −5.4a −5.4 0.039 23
-UAACC −3.9 −3.0 0.041 230

All experiments were performed at 30 °C and pH 7.2. All substrates contained a 2′-deoxyribose substitution at the cleavage site (position –1) to prevent cleavage. Ktert values were obtained by comparison of docked and undocked substrates as described in the Materials and Methods, with oligonucleotide substrates undocked by the introduction of a 2′-methoxyribose substitution at position –3 (26, 35, 55). Δ ΔGbp values were obtained by comparison of the affinity of the CCUCdTAAACC or CCUCdTUAACC with CCUCdTA.

a

Value from Table 1 included for comparison.