The Circular dichroism spectra analysis of rNSs showed a minimum in the range of 215-223 nm (Fig. 2B) . The intrinsic fluorescence emission spectrum showed a maximum at 338 nm upon excitation at 280 nm (Fig. 2C) . rNSs contains five tryptophans and eleven tyrosines which are buried as is apparent from the emission fluorescence maximum at 338 nm. These results demonstrate that rNSs is in a folded conformation. The thermal stability of rNSs monitored by CD spectroscopy revealed that it is a stable protein with a Tm of 65uC (Fig. 2D ).