Comparison of conformational stability of MsEis and RvEis proteins in the presence of different denaturants.

Intrinsic tryptophan fluorescence spectra of MsEis and RvEis proteins in the presence of increasing concentration of GdmCl (Panel A), urea (Panel C) and at increasing temperature from 25°C to 100°C (Panel E). Unfolding of MsEis and RvEis proteins measured in terms of changes in emission wavelength maxima in the presence of GdmCl (Panel B), urea (panel D) and temperature (Panel F). The values corresponding to native Eis without treatment were considered as 100%. Fitting of the values obtained from emission maxima were done by using equations with OriginPro 8.0 software.