Overview
This technical note investigates how the full spectrum capabilities of the SUPR-DSF make it easy for researchers to measure unfolding curves for proteins without tryptophan. The protein we are using for this study is Protein A, a 42 kDa surface protein originally found in the cell wall of the bacteria Staphylococcus aureus. It has found several uses in biochemical research due to its ability to bind to the Fc region of immunoglobulins. Protein A does not contain any tryptophan residues but does contain four tyrosine residues. The tyrosine fluorescence will be utilized to analyze Protein A’s thermal stability on the SUPR-DSF.
