Effect of small molecules on the thermal stability of MglA or SspA and their effect on protein-protein interaction.

The thermal stabilization of each protein was evaluated using fluorometry with an average of 40 µM of ligand.
The chemicals were tested in vivo using the two-hybrid system at concentrations between 0.05–250 µM.
1ΔTm was calculated as the difference in the transition temperature between the proteins in the absence (MglA = 48.7°C; SspA = 42.4°C) and presence of a given chemical. The results were averaged from duplicates.
2β-galactosidase activity (expressed as arbitrary units) as a result of pBR-mglA-ω and pACTR-sspA-Zif interaction is expressed as the decrease in the activity in the presence of the chemicals, compared to the control without chemicals after 180 min. The assay was performed three times, each in duplicates.