Table 2. Parameters of MutS binding to DNA, ATP hydrolysis and nucleotide exchange in ATPase domain of protein.

Duplex number (X/Y)a	Initial rates (v 0) of ATP hydrolysis by MutS		Dissociation constants (K d) of MutS complexes with DNA	Rate constants of ADP exchange (k off mant-ADP) in ATPase domain of MutS
	v 0, nM·s−1	Rel. v 0 b	K d, nM	k off, s−1	Rel. k off c
MutS without DNA	0.37±0.018	1.0	-	0.012±0.001	1.0
I (G/C)	0.77±0.069	2.1	32±3.3	0.047±0.001	3.9
II (G/T)	0.75±0.073	2.0	7±1.5	0.28±0.013	23.0
III (G/Tg)	0.66±0.036	1.8	44±2.3	0.037±0.015	3.0
IV (A/Tg)	0.69±0.011	1.9	25±3.0	0.025±0.001	2.1

^aVariable nucleotide pair.

^bThe ratio of v ₀ of ATP hydrolysis by MutS in the absence or in the presence of duplexes I–IV to v ₀ of ATP hydrolysis by MutS in the absence of DNA.

^cThe ratio of rate constant of mant-ADP dissociation from its complex with MutS (k _off ^mant-ADP) in the absence or in the presence of duplexes I–IV to k _off ^mant-ADP in the absence of DNA.

The error of the mean indicates a SEM.