Figure 7From: Conformational changes and loose packing promote E. coli Tryptophanase cold labilityThe β sheet at the non-catalytic interface is formed by two anti parallel β strands from subunits A (shown in blue) and C (shown in green). This hydrophobic core is not exposed to the solvent and accounts for the dissociation of E. coli Trpase to dimers only.Back to article page