Typical folded proteins have a stability ranging from 7 to 15 kcal/mole at 37°C. Stability is a measure of the equilibrium between the folded (F) and unfolded (U) forms of the protein, with the unfolded form having a greater free energy (see Figure Q4-20). For a protein with a stability of 7.1 kcal/mole, calculate the fraction of protein that would be unfolded at equilibrium at 37°C. The equilibrium constant (Keq) is related to the free energy (?G°) by the equation Keq = 10-?G°/1.42.

Typical folded proteins have a stability ranging from 7 to 15 kcal/mole at 37°C. Stability is a measure of the equilibrium between the folded (F) and unfolded (U) forms of the protein, with the unfolded form having a greater free energy (see Figure Q4-20). For a protein with a stability of 7.1 kcal/mole, calculate the fraction of protein that would be unfolded at equilibrium at 37°C. The equilibrium constant (Keq) is related to the free energy (?G°) by the equation Keq = 10-?G°/1.42.

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Typical folded proteins have a stability ranging from 7 to 15 kcal/mole at 37°C. Stability is a measure of the equilibrium between the folded (F) and unfolded (U) forms of the protein, with the unfolded form having a greater free energy (see Figure Q4-20). For a protein with a stability of 7.1 kcal/mole, calculate the fraction of protein that would be unfolded at equilibrium at 37°C. The equilibrium constant (Keq) is related to the free energy (?G°) by the equation Keq = 10-?G°/1.42.



Answer: 1/100,000


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