Le Vendredi 14 Mars 2014 13:37 CET, Anita P <crystals...@gmail.com> a écrit:
Anita, If one of the partners is indeed more or less unfolded before interaction, then you should see a negative DeltaS upon complex formation. Practically, I would try first putting the unfolded protein in the cell and the folded one in the syringe in view of possible solubility problems with an "incorrectly" folded protein. Alanine scanning ? Yes on the paper, but may be less feasible in practice due to the amount of material to prepare. Good luck Philippe Dumas > Hello everyone, > > I have a query for the scientists working on protein-protein interaction. > It is known that some proteins exist in unfolded or molten globule state > and attain structure on interaction with other folded proteins. > Many a times, it is difficult to obtain the structure of these complexes. > > Is it possible to quantitatively determine the thermodynamics of > interaction between an unfolded protein and a folded protein using ITC? > Later may be perform an alascan to determine the residues of the unfolded > partner involved in the interaction. > > Please share your ideas > > cheers > Anita
