Applications of Differential Scanning Fluorometry and Related Technologies in Characterization of Protein-Ligand Interactions.

Abstract

Differential scanning fluorometry (DSF) is an efficient and high-throughput method to analyze protein stability, as well as detect ligand interactions through perturbations of the protein's melting temperature. The method monitors protein unfolding by observing the fluorescence changes of a sample, whether through an environmentally sensitive fluorophore or by intrinsic protein fluorescence, while a temperature gradient is applied. Here, we describe in detail how to develop and optimize DSF assays to identify protein-ligand interactions while exploring different buffer and additive conditions. Analysis of the data and further applications of the method are also discussed.

Authors

Baljinnyam, Bolormaa; Ronzetti, Michael; Yasgar, Adam; Simeonov, Anton;

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