I am interested to determine affinities of a highly disordered protein derived from a coregulator to different nuclear receptor heterodimers. The MST method was very efficient to measure these affinities, with high reproducibility. Data are in perfect agreement with structural and functional data. I could not obtain such accurate data before with other methods, like fluorescence anisotropy. MST experiments consume very low amount of protein and are rapid to run, which is especially interesting when you want to do a number of runs in same conditions, but different interacting proteins. The support from NanoTemper Technologies in Brazil is very helpful and very competent. I will continue to use MST for other types of interactions (protein-peptide, protein-ligand, protein-protein).
Dr. Albane le Maire