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TOPIC: Linked reactions

Linked reactions 05 Oct 2005 02:00 #1

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Hi all,

I am trying to identify a conformational change upon Analyte binding to Ligand. I know that different dissociation rates with different injecting times at a constant analyte concentration is the method to resolve this question. But the A-L interaction does not reach steady-state even at high analyte concentrations (200 nM) even at long injection times.

Is there any solution?

thanks in advance and good luck with your experiments

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Linked reactions 05 Oct 2005 02:00 #2

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Try to calculate if your goal is feasable.

You can calculate the Req

Req = (ka . C / ka . C + kd) Rmax

You can estimate the time to reach equilibrium

teq = -ln(1-@)/(ka . C + kd)

where teq is the time to equilibrium and @ is the fraction of reached equilibrium, typical 95% thus 0.95

Arnoud

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