That is a very interesting question, which I would request the seniors out there to give their insights on.
I was imagining that a recombinant purification of an unfolded partner would aggregate which would cause trouble in ITC. Am I correct in this theory? Would love to have more insights. thanks in advance Anita On Fri, Mar 14, 2014 at 7:18 PM, <rkha...@ccny.cuny.edu> wrote: > Hi, > > I think the experiment is doable, but how would you decouple > protein-protein interaction from folding of the unfolded > protein due to protein interaction? > > Reza > > Reza Khayat, PhD > Assistant Professor > The City College of New York > Department of Chemistry, MR-1135 > 160 Convent Avenue > New York, NY 10031 > Tel. (212) 650-6070 > > > ---- Original message ---- > >Date: Fri, 14 Mar 2014 18:07:48 +0530 > >From: CCP4 bulletin board <CCP4BB@JISCMAIL.AC.UK> (on behalf > of Anita P <crystals...@gmail.com>) > >Subject: [ccp4bb] ITC with unfolded proteins > >To: CCP4BB@JISCMAIL.AC.UK > > > > 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 >
