Hi everyone,
I am working on a viral protein and its interaction with sugars. From the literature, it seems that the interaction is in the mM range (around 20 mM). I am using ITC, but unfortunately, even when I try different concentrations of protein and ligand, the results are not promising. Do you know of a better technique to evaluate this type of interaction?
Tryptophan fluorescence of the protein, surface plasmon resonance, biolayer interferometry, microscale thermophoresis, differential scanning fluorescence, differential scanning calorimetry.
Dear @luca
As Adam suggest probably tecniques ad BLI, SPR or ELiSA have to work in some way. In my experience those tecniques work well in the uM range, but i never test it in the mM.
2D NMR using 15N labelling samples could be also able to detect very weak interactions thanks the high sensitivity of the chemical shift but it is more sample and time consuming respect than the other tecniques.
best regards
Manuele
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