Final Answer:
The correct expression for ΔG'o for the transition observed in the experiments described in the passage is ΔG'o = ΔH'o - TΔS'o.
Step-by-step explanation:
In the field of biochemistry, the Gibbs free energy change (ΔG) for a reaction under standard conditions is expressed as ΔG'o = ΔH'o - TΔS'o, where ΔH'o is the standard enthalpy change, T is the absolute temperature in Kelvin, and ΔS'o is the standard entropy change. The transition mentioned in the passage involves the unfolding of proteins, resulting in a change in the standard enthalpy and entropy.
The enthalpy change (ΔH'o) reflects the heat absorbed or released during the unfolding process, and the entropy change (ΔS'o) represents the disorder or randomness change in the system. For protein unfolding, ΔH'o is typically positive as energy is needed to break the molecular forces stabilizing the folded structure. Meanwhile, ΔS'o is negative since the unfolded state is often more disordered than the folded state. As a result, the overall ΔG'o for protein unfolding is influenced by both factors.
To calculate ΔG'o, substitute the values of ΔH'o, T, and -ΔS'o into the equation. The negative sign with ΔS'o ensures that the entropy term subtracts from the enthalpy term. This thermodynamic expression quantifies the feasibility of the protein unfolding process under standard conditions, providing valuable insights into the spontaneity of the transition observed in the experimental setting.