Figure 4: Introduction of conformational flexibility results in cells with a switching phenotype and allosteric proteins.
From: Design of protein switches based on an ensemble model of allostery
(a) Maltose-dependent fold increase in Amp resistance for cells expressing the indicated proteins at 18 and 37 °C. (b) Maltose-dependent fold increase in Amp resistance for cells expressing the indicated proteins grown in media with the indicated initial pH. The MICAmp ratio (+maltose/−maltose) was calculated using the median MICAmp value from three independent trials. (c) Maltose-dependent fold increase in initial rate of nitrocefin hydrolysis enzymatic activity of c4 and c4-3G at 18 and 37 °C. (d) Maltose-dependent fold increase in initial rates of nitrocefin hydrolysis enzymatic activity of c4 and c4-3hx at pH 6 and 8, respectively. Average rates were calculated from three independent trials.
