Comparison and mutual verification of two microthermal techniques for quantitative detection of protein-compound interactions
The technologies are used to research the mechanism of molecular interaction by detecting the characteristics of the interaction between protein and other substances,such as affinity constant.The isothermal titration calorimetry(ITC)and micro scale thermophoresis(MST)are widely used in the quantitative detection of the interaction between moleculars.In this article,the two techniques are used for the quantitative detection of the interaction between phosphoglycerate kinase(P1)and terazosin hydrochloride(TZ),and the experimental results are successfully obtained and mutually verified.Meanwhile,the pros and cons of the two detection techniques are discussed in depth,which provides new ideas for the selection of detection methods under different conditions.
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