Selected article for: "isothermal titration calorimetry and ITC isothermal titration calorimetry"
Author: David N. Frick; Rajdeep S. Virdi; Nemanja Vuksanovic; Narayan Dahal; Nicholas R Silvaggi
Title: Variable Macro X Domain of SARS-CoV-2 Retains the Ability to Bind ADP-ribose
  • Document date: 2020_4_2
    • ID: 02q9y011_16
    Snippet: Isothermal Titration Calorimetry (ITC)-Binding of ADP-ribose to the SARS-CoV-2 macro X domain was measured using a Nano ITC (TA Instruments). Before starting the measurement, samples of both ligand and protein were diluted in 10 mM MOPS, 150 mM NaCl (pH 7) and were degassed at 400 mmHg for 30 minutes. Measurements were taken at 20 °C by injecting 2.0 µl aliquots of 500 µM ADP-Ribose (Sigma) to 50 µM protein (175 µl initial volume) with 250 r.....
    Document: Isothermal Titration Calorimetry (ITC)-Binding of ADP-ribose to the SARS-CoV-2 macro X domain was measured using a Nano ITC (TA Instruments). Before starting the measurement, samples of both ligand and protein were diluted in 10 mM MOPS, 150 mM NaCl (pH 7) and were degassed at 400 mmHg for 30 minutes. Measurements were taken at 20 °C by injecting 2.0 µl aliquots of 500 µM ADP-Ribose (Sigma) to 50 µM protein (175 µl initial volume) with 250 rpm stirring rate. Using Nano-Analyze Software (v. 3.11.0), data were fitted by non-linear regression to an independent binding model. Briefly, after baseline correction, background heats from ligandto-buffer titrations were subtracted, and the corrected heats from the binding reaction were used to find best fit parameters for the stoichiometry of the binding (n), free energy of binding (DG), apparent enthalpy of binding (DH), and entropy change (DS). Dissociation constants (Kd) were calculated from the DG.

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