If your are talking about proteins or protein subunits, this means that you are 
making polymers of nY, and Y becames the monomer. So in this case, I will not 
consider Y as an impurity. 
If I get you right, then size exclusion chromtography is good option to 
separate the monomers from the bigger polymers.
Another way to do that, in my opinon, is that if you have a good estimate of 
the stoichometry between the monomers and polymers (and hence concentration of 
monomer in the cell), then run a refrence ITC with same monomer concetrate and 
this will automatically subtract the influence of Y component. 

I hope this give the slightest hint!! 

--- On Tue, 8/24/10, Francis E Reyes <francis.re...@colorado.edu> wrote:

From: Francis E Reyes <francis.re...@colorado.edu>
Subject: [ccp4bb] offtopic: effect of compound impurities on ITC?
Date: Tuesday, August 24, 2010, 11:11 AM

Hi All

I'm curious the effect of small impurities in commercially synthesized 
compounds on ITC and its analysis. Say if compound Y is the high affinity 
binder, but you make a derivative that differs from a single functional group 
from Y (you used Y to make this new compound) and you never are able to 
completely get rid of Y. How does this affect the analysis of determining the 
derivative's affinity by ITC?

References or personal experience is appreciated!


Francis E. Reyes M.Sc.
215 UCB
University of Colorado at Boulder

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