Hi,
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!!
Ahmed.
--- 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?
To: CCP4BB@JISCMAIL.AC.UK
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!
F
---------------------------------------------
Francis E. Reyes M.Sc.
215 UCB
University of Colorado at Boulder
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