Additionally, by plotting the apparent enthalpy of binding versus the ionization enthalpy of each buffer and seeing a slope of approximately zero, we determined that upon binding the various DmsAL peptides at pH 8.0, the DmsD::DmsAL complexes do not have a net gain or loss of protons for any of the peptides.
The enthalpy and entropy values were calculated by plotting the ln(E) values against the reciprocal reaction temperature.
Data were analyzed by plotting the observed ellipticity as a function of temperature and fitting for the melting point transition (Tm) and the enthalpy (Δ Hm) according to eq 1.
van't Hoff plots were generated by plotting the Tm versus the concentrations of non-self-complementary three molecular strands according to a previous method: 2where R is the gas constant 1.987 cal mol 1 K–1, Ct is the total concentration of each 3WJs, and Δ H° and Δ S° are enthalpy and entropy changes, respectively.
To probe the enthalpy entropy compensation effect for the binding of the SAHA analogues to HDAC8, we plotted the experimentally determined values of Δ H ° and Δ G ° as a function of TΔ S °. Figure 6 shows representative enthalpy entropy compensation plots for the binding of SAHA (left panel) and C6-cSAHA (right panel) to HDAC8.
The thermodynamic parameters are analyzed by using the enthalpy method.
When [S] approaches to 1/v, ∆G L is dominated by the enthalpy term.
Interestingly, this interaction was driven mainly by entropy since the enthalpy contribution was measured to be very small.
A salt, a salt-complex combination, or a simple physical mixture can be differentiated by measurement of the enthalpy changes of neutralization, which ranges usually in the area of −55 to −66 kJ/mole for the salt formation to less than −5 kJ/mole for the change in complexation enthalpy to no changes in enthalpy for a physical mixture (1995).
The result of van't Hoff plot suggests that the enthalpy is dominant for the complexation of tacrolimus with DM‐β‐CyD.
