Figure 2From: Conformational changes and loose packing promote E. coli Tryptophanase cold labilityTime dependence of cold inactivation and dissociation of wt Trpase and C298S and W330F mutants incubated at 2°C in Tricine-KCl buffer at pH 7.5. Activity was measured by a spectrophotometric method with the chromogenic substrate analog, S-(o-nitrophenyl)-L-cysteine (SOPC); Protein concentration: 1.0 mg/ml.Back to article page