$A$ protein undergoes reversible thermal denaturation from its initial state $N$ to denatured state $D$ according to $N \rightleftharpoons D$. At $60 ^\circ C$, the concentrations of both $N$ and $D$ are equal at equilibrium, and the standard enthalpy change of denaturation is $666 \text{ kJ mol}^{-1}$. The standard entropy change ($\Delta S^\circ$ in $\text{kJ K}^{-1} \text{mol}^{-1}$) of the protein upon denaturation at $60 ^\circ C$ is closest to

  • A
    $2.0$
  • B
    $2000.0$
  • C
    $333.0$
  • D
    $11.1$

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