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. Author manuscript; available in PMC: 2010 Jan 4.
Published in final edited form as: Biochemistry. 2008 Dec 30;47(52):13754–13763. doi: 10.1021/bi801666c

Table 2.

Properties of AGT-DNA Complexes

DNA
Length
(bp)
Mr
(Saturated
Complex)a
Stoichiometry Sapp
bp/protein
K/M ω K•ω
11 5.08 ± 0.24
× 104
2.05 ± 0.11a
1.99 ± 0.15b
5.36 ± 0.31a
5.52 ± 0.38b
1.69 ± 0.19 × 103 c 45.9 ± 6.0c 7.75 ± 1.92 × 104
12 - 2.91 ± 0.14b 4.13 ± 0.21b 4.08 ± 1.12 × 103 c 48.0 ± 5.5c 1.96 ± 0.78 × 105
14 - 2.94 ± 0.10b 4.75 ± 0.12b 6.11 ± 0.96 × 103 c 52.3 ± 5.1c 3.18 ± 0.82 × 105
16 9.71 ± 0.17
× 104
3.94 ± 0.08a
3.98 ± 0.01b
4.06 ± 0.08a
4.04 ± 0.02b
1.25 ± 0.22 × 104 c 105.2 ± 18.8c 1.31 ± 0.47 × 106
18 - 3.82 ± 0.24b 4.70 ± 0.18b 4.23 ± 0.72 × 103 c 85.7 ± 11.6c 3.59 ± 1.10 × 105
21 - 5.06 ± 0.20b 4.15 ± 0.17b 6.07 ± 1.80 × 103 c 92.6 ± 25.1c 5.62 ± 3.21 × 105
22 - 4.58 ± 0.24b 4.80 ± 0.24b 3.80 ± 0.95 × 103 c 68.3 ± 13.5c 2.58 ± 1.16 × 105
24e - 5.93 ± 0.25b 4.05 ± 0.18b 2.31 ± 0.36 × 103 c 83.1 ± 13.2c 1.92 ± 0.61 × 105
24f - 6.01 ± 0.20b 3.99 ± 0.14b 4.01 ± 1.78 × 103 c 110.1 ± 23.2c 4.41 ± 2.89 × 105
26 1.37 ± 0.41
× 105
5.64 ± 0.18a
5.50 ± 0.16b
4.60 ± 0.18a
4.72 ± 0.14b
8.18 ± 2.52 × 103 c 93.5 ± 26.5c 7.64 ± 4.53 × 105
30 1.49 ± 0.34
× 105
6.08 ± 0.16a
6.43 ± 0.13b
4.93 ± 0.13a
4.66 ± 0.11b
9.71 ± 2.03 × 103 c 64.7 ± 15.3c 6.28 ± 2.79 × 105
41 - 9.01 ± 0.24b 4.55 ± 0.13b 1.87 ± 0.45 × 103 c 145.0 ± 37.0c 2.71 ± 1.35 × 105
148 5.66 ± 0.14
× 105
21.76 ± 0.65a 6.80 ± 0.21a 8.23 ± 1.51 × 103 d 53.5 ± 22.1d 4.40 ± 2.62 × 105
208 8.05 ± 0.33
× 105
31.04 ± 1.54a 6.70 ± 0.35a 7.87 ± 0.82 × 103 d 63.6 ± 16.6d 4.95 ± 1.82 × 105
2686 1.05 ± 0.51
× 107
406.3 ± 23.7a 6.61 ± 0.41a 8.52 ± 0.96 × 103 d 22.6 ± 3.7d 1.92 ± 0.53 × 105
a

Determined by sedimentation equilibrium analysis. The error ranges are 95% confidence limits.

b

Determined by EMSA-serial dilution analysis. The error ranges are 95% confidence limits.

c

Determined by scatchard analysis of EMSA data, using binding densities calculated from serial dilution analysis.

d

Determined by scatchard analysis of sedimentation equilibrium data, using binding densities calculated from Mw of the protein-DNA complex.

e

dG24•dC24

f

dA24•dT24