If the following is not deleterious to your protein and its function you
could introduce mutations that prevent dimerization.
~Jeff
> I have a similar case, where in there are multiple binding sites on the
> protein for the ligand and ligand induces dimerization.So it is not
> helpful
> even if I
n board [CCP4BB@JISCMAIL.AC.UK] de la part de Ramesh V
[ramesh.c...@gmail.com]
Envoyé : vendredi 18 juillet 2014 14:42
À : CCP4BB@JISCMAIL.AC.UK
Objet : Re: [ccp4bb] ITC with heterogeneous protein
I have a similar case, where in there are multiple binding sites on the protein
for the ligand and
I have a similar case, where in there are multiple binding sites on the
protein for the ligand and ligand induces dimerization.So it is not helpful
even if I separate the monomer and dimer.
If I titrate the dimer with ligand, the stoichiometry will completely
change? Any suggestions will be helpful
Hi Sajid,
*Assuming* you have one site per monomer (rather than, say, one site per
dimer), and *assuming* each binding event is completely independent ( I.e
no co-operativity), you might just get away with running the experiment
with the heterogeneous material.
However, you might not be able to c
Dear Sajid
If the binding site of your ligand is remote from the dimerization interface,
it should normally not be a problem. You will bind two ligands for a dimer and
one ligand for a monomer and you should be able to fit the isotherm with one
unique site even in presence of a mix of monomers
Dear Sajid,
one first problem in your study is how-to adress if the deltaH mesured is
caused by the ligand interaction, or by the modification of dimer-monomer
equilibrium.
You have to well caracterise your system dimer-monomer. One other problem is
about the accessibility of the interaction si