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A two-cent suggestion – a sedimentation velocity analytical ultracentrifugation (SV-AUC) experiment at different concentrations could be very useful in defining these species and getting a pulse on the Kds of association.
Kushol
Kushol Gupta, Ph.D.
Research Assistant Professor, Department of Biochemistry and Biophysics
Director, Johnson Foundation Structural Biology and Biophysics Core
Perelman School of Medicine at The University of Pennsylvania
kgu...@upenn.edu / 267.259.0082 / www.stwing.upenn.edu/~kgupta
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<NT_C.zip>
I just happen to be studying concentration effects right now (non-constant structure factors). Your data sure look like a classic case of monomer with charge repulsion. I have superimposed most dilute curve on most concentrated curve. Neglecting the small upturn at lowest angle, there is always a big dip at lower angles which gets bigger with concentration. Ignoring the solvent, you can think of the proteins as if they were ideal gas atoms. The dip below the dilute scattering curve is related to the compressibility of the "protein gas" which gets harder to compress as the particles get closer together. The first peak above the dilute curve is due to the separation between proteins in solution. This moves to lower angle as you get more concentrated. Sorry that none of this probably helps your situation, but it may be helpful for you to see what is due to concentration effect: the concentrated curve rises above the dilute curve around q = 0.7 nm-1, but this is probably not evidence of increasing oligomers, but rather a natural effect of interparticle interference.
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