Application Note: nanoDSF Thermal Unfolding Analysis of Proteins Without Tryptophan Residues
25 April 2016

This study demonstrates the ability of the Prometheus NT.48 to analyze protein stability in samples that do not contain any tryptophan residues. Fluorescence of the amino acid tryptophan, which is usually located within the hydrophobic core of a protein, is highly sensitive to changes in its immediate environment. By detecting the changes in tryptophan fluorescence intensity and the emission peak shift, the melting temperature Tm of proteins can be determined in a dye-free approach. The results show that the Prometheus NT.48 by NanoTemper Technologies is capable of monitoring fluorescence emission changes in samples without tryptophan residues, and thus can determine thermal stability of these proteins.