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. Author manuscript; available in PMC: 2012 May 12.
Published in final edited form as: J Med Chem. 2011 Apr 19;54(9):3260–3267. doi: 10.1021/jm101554k

Table 2.

Protein denaturation summary for interactions of vaccinia virus D4 with small molecule compoundsa

Hit Tm (°C) ΔTm (°C) Hit Tm (°C) ΔTm (°C)
DMSO mock 38.4 ± 1.6 0.0 14 48.4 ± 6.0 10.0
1 34.7 ± 1.5 −3.7 15 44.3 ± 3.7 4.9
2 36.4 ± 0.4 −2.0 16 35.2 ± 2.0 −5.0
3 35.1 ± 0.7 −3.3 17 35.1 ± 1.8 −1.7
4 35.2 ± 1.0 −3.2 18 34.3 ± 0.7 −4.1
5 36.4 ± 1.3 −2.0 19 38.3 ± 1.3 −0.1
6 36.9 ± 1.0 −1.5 20 34.9 ± 1.3 −3.5
7 36.3 ± 0.9 −2.1 21 34.8 ± 1.5 −3.6
8 32.2 ± 0.3 −6.6 22 34.7 ± 0.4 −3.7
9 51.4 ± 9.1 13.1 23 33.2 ± 0.3 −4.9
10 53.3 ± 1.5 14.9 24 35.4 ± 0.4 −3.2
11 36.3 ± 0.5 −1.5 25 35.9 ± 0.8 −2.5
12 35.0 ± 0.4 −3.4 26 33.6 ± 2.0 −4.8
13 36.5 ± 1.2 −1.9 27 43.0 ± 3.0 4.6
a

Experiments were performed using 4 μM D4 in the presence or absence of 50 μM compounds in 25 mM Tris, pH 7.2, 0.15 M NaCl, 5 mM ZnCl2, and 1 % DMSO. Tm values are shown ± SD from at least three independent experiments (n=3-5), with thermal shift (ΔTm) values obtained by the subtraction of the untreated DMSO mock.