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
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
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
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
@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 ligand induces
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
