Fig. 5: Mutational effects on ligand binding and fluorescence enhancement by RhoBAST.
From: Structural mechanisms for binding and activation of a contact-quenched fluorophore by RhoBAST
a Mutants of RhoBAST WT presumed to disrupt certain tertiary interactions are mapped to its secondary structure. Residues are numbered corresponding to the L2-U1 crystallization construct, and secondary structures are shown in gray for comparison. b ITC analysis of ligand binding affinity of all the mutants. (“*”means no binding; “#” means weak binding) (mean ± s.d., n = 3). c Fluorescence of all the RhoBAST mutants in the presence of TMR-DN are normalized to the WT (mean ± s.d., n = 3). Source data for panels b–c are provided as a Source data file.
