Math Problem Statement

Consider the folding of a globular protein at 35°C. You perform a protein folding experiment and determine that ΔG’= -3.3 kJ/mol. You find that at the end of the experiment, 1 𝝁M is in the folded state and 4 𝝁M of the protein is in the unfolded state. Calculate ΔG°’

Solution

To calculate \Delta G^\circ', we use the relationship between ΔG\Delta G' and \Delta G^\circ':

\Delta G' = \Delta G^\circ' + RT \ln(Q)

where:

  • ΔG\Delta G' is the free energy change under experimental conditions, which is given as 3.3kJ/mol-3.3 \, \text{kJ/mol}.
  • \Delta G^\circ' is the standard free energy change we want to find.
  • RR is the universal gas constant, 8.314×103kJ/(mol\cdotpK)8.314 \times 10^{-3} \, \text{kJ/(mol·K)}.
  • TT is the temperature in Kelvin (35°C = 308 K).
  • QQ is the reaction quotient, which is the ratio of the concentrations of the unfolded and folded states.

Step 1: Calculate the reaction quotient QQ.

The reaction quotient QQ is given by:

[ Q = \frac{[\text{unfolded}]}{[\text{folded}]} ]

In this experiment:

  • [folded]=1μM[\text{folded}] = 1 \, \mu M
  • [unfolded]=4μM[\text{unfolded}] = 4 \, \mu M

So:

Q=4μM1μM=4Q = \frac{4 \, \mu M}{1 \, \mu M} = 4

Step 2: Substitute values into the equation.

-3.3 \, \text{kJ/mol} = \Delta G^\circ' + (8.314 \times 10^{-3} \, \text{kJ/(mol·K)})(308 \, \text{K}) \ln(4)

Calculate RTln(4)RT \ln(4):

  • ln(4)1.386\ln(4) \approx 1.386
  • RTln(4)=(8.314×103)(308)(1.386)RT \ln(4) = (8.314 \times 10^{-3})(308)(1.386)

RTln(4)(2.561kJ/mol)RT \ln(4) \approx (2.561 \, \text{kJ/mol})

Step 3: Solve for \Delta G^\circ'.

-3.3 \, \text{kJ/mol} = \Delta G^\circ' + 2.561 \, \text{kJ/mol}

\Delta G^\circ' = -3.3 \, \text{kJ/mol} - 2.561 \, \text{kJ/mol}

\Delta G^\circ' \approx -5.861 \, \text{kJ/mol}

So, the standard free energy change \Delta G^\circ' is approximately 5.86kJ/mol-5.86 \, \text{kJ/mol}.

Would you like further details or have any questions?

Here are 5 related questions:

  1. How does temperature affect the folding of a protein and its \Delta G^\circ'?
  2. What does a negative \Delta G^\circ' indicate about a protein's folding stability?
  3. How would the calculation change if the concentration of the folded and unfolded states were reversed?
  4. What is the significance of the reaction quotient QQ in determining ΔG\Delta G'?
  5. How do different values of \Delta G^\circ' relate to the equilibrium constant KK for protein folding?

Tip: Always check the units in thermodynamic calculations to ensure consistency, especially when working with temperatures and gas constants.

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Math Problem Analysis

Mathematical Concepts

Thermodynamics
Reaction Quotient
Gibbs Free Energy

Formulas

ΔG' = ΔG°' + RT ln(Q)
Q = [unfolded] / [folded]

Theorems

Gibbs Free Energy Equation

Suitable Grade Level

Undergraduate