Near UV CD, ANS-fluorescence spectra, and DLS profile show structural stabilization and elongated conformation of the proteins. A. Near UV CD signal recorded from 300 nm to 250 nm, shows negative signal for PcrV and PcrG-PcrV at 285 nm and 287 nm, respectively. PcrG shows absence of tertiary structure signal. B. ANS-binding profile of proteins was scanned from 400 nm to 600 nm. Both PcrV and PcrG-PcrV exhibit a blue-shift in the ANS-binding spectra, showing the presence of solvent exposed hydrophobic patches in the proteins. However, the spectrum of PcrG was similar to that of ANS. C. DLS profiles of PcrV, PcrG-PcrV and LcrV, LcrG-LcrV with corresponding hydrodynamic diameters, confirm an elongated conformation of the proteins.