So we do microscale thermophoresis (MST) with labeled protein and labeled DNA. Typically standard titrations are easily performed and there are no problems. However, with some experimental compounds we seem to get "never ending" isotherms that won't ever reach saturation. In other words, we can keep increasing the amount of ligand but we never get saturation. The signal/noise is just fine in most of these cases. Our standard buffer conditions are 8-20 mM phosphate buffer with 20-200 mM KCl or NaCl, pH 7. The ligand is typically dissolved at 10 mM in DMSO as our stock, so DMSO ranges from
Mo Yang - thanks for the response. Non-specific adsorption was what I was thinking it could be but have not seen any literature showing that to be the case. Do you have a reference to any studies investigating this phenomenon?
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