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. 2013 Sep 11;288(43):31105–31114. doi: 10.1074/jbc.M113.508606

TABLE 1.

Thermostability and time course activity data of DENV4 FL and RdRp proteins

Protein melting temperatures (Tm; °C) were determined by thermofluorescence as described under “Experimental Procedures.” Each protein was measured in triplicate wells. Protein activity was measured in a de novo initiation FAPA assay. Results shown are the average percentage of activity compared with DENV4 FL WT NS5 protein derived from average RFU obtained for each protein from at least three independent experiments. All data points were performed in triplicate wells.

De novo initiation activity
Thermofluorescence, Tm
1 h 2 h 3 h
% °C
FL WT 100 100 100 37.5
RdRp264–900 242.5 ± 21.7 216.7 ± 16.5 174.9 ± 9.6 44
RdRp266–900 293.4 ± 42.2 267.4 ± 20.0 244.8 ± 22.0 42
RdRp268–900 115.4 ± 11.1 109.2 ± 8.7 87.2 ± 14.6 43
RdRp270–900 108.9 ± 15.3 117.3 ± 9.4 109.8 ± 22.5 42
RdRp273–900 82.0 ± 13.0 80.2 ± 18.0 77.2 ± 21.5 38