To compare the changes in thermal stability of wild-type protein D and mutant protein.
Technical difficulties：
▇The traditional dye-based DSF method resulted in unclear differences and poor peak quality in the spectra of the
wild-type and mutant proteins.
Solution：
▇The label-free Nano-DSF, based on the intrinsic tryptophan fluorescence shift during protein unfolding, quickly provided
high-quality results. ▇The spectra intuitively displayed the relative thermal stability of each protein.
23 Feb 
