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The value was divided by the molar amount of TbTIM injected in order to obtain the binding enthalpy that was −0.32 kcal/mol.
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With SA on the other hand, the binding that was entropy dominated at lower temperatures became enthalpy dominated at higher temperature.
The titration of U2A′ with SNF shows a very large apparent enthalpy of binding that is temperature-dependent, indicating a change in heat capacity (Δ C p ) associated with binding.
The binding phenomena analyzed from isothermal titration calorimetry showed exothermic binding for both compounds that was favoured by negative enthalpy and positive entropy changes typical of intercalative binding.
In this [K+] range, both specific and non-specific binding are enthalpy-driven, with large negative enthalpy, entropy and heat capacity changes and binding constants that are insensitive to [K+].
The binding of the iminium was clearly enthalpy driven (ΔH = −6.148 kcal/mol) with a small entropy contribution (TΔS = 0.320 kcal/mol), while that of the alkanolamine form was driven by enthalpy changes (−2.557 kcal/mol) and a strong entropic component (TΔS = 5.125 kcal/mol) that was favorable to the binding.
Presumably, the Y313A mutation should introduce negligible change in binding enthalpy, given that Y313 is always involved in hydrogen bonding prior and after the binding of L-arginine.
The binding of f-IPI (3a) to 5′-ACGCGT-3′ via the stacked dimer motif was balanced between enthalpy and entropy, and that was quite different from the enthalpy-driven binding of its monoamino parent f-IPI (1).
Thermodynamic studies showed that binding enthalpies were endothermic; the nano-complex formation was entropically driven.
However, with this RNA, the positive and unfavorable binding enthalpy was compensated by a significant change in entropy.
For alginate chitosan complexes, the binding enthalpy has been seen to be −3.49 kJ/mol.
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