I used Microscale thermophoresis(MST, from Nanotemper) to determine the constant of dissociation (Kd) between a protein (20 nM) and a ligand (1:2 serial dilution from 50 μM to 1.5 nM). I ran the analysis at 25 and 37 °C and I got:
25 °C: 1.8 × 10e–5 ± 4.6 × 10e–6 μM
37 °C: 1.8 ± 0.4 μM
The second measurement looks fine to me; the first, a bit meaningless.
Is there a way to assess if a Kd value is correct? Does the first value mean that there is no adsorption?
Thank you
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