Please show all of your work. Thank you! There is also no other information on t

Question

Please show all of your work. Thank you! There is also no other information on the problem. For part A though, the Kd should remain the same. I mainly need help with part B. Thank you!

An artificial myoglobin our lab recently designed has two independent O_2 binding sites. The experimentally observed K_d for the first site was 600 nM. (a) Estimate the observed K_d for the second. (b) The Delta G_folding for the protein in the absence of O_2 is -5.5 kcal/mol. Assuming the unfolded protein cannot bind O_2, what is the Delta G_folding in O_2 -saturated solution (2 mM)?

Explanation / Answer

The Delta G folding state is or unfolding the magnitude does not changes. The Gibbs free energy change depends on Delta H0 and Delta S0, depending on the use of them in folding or unfolding state.

Delta G0= Delta H0 - Delta S0.

Also we can use the equation like  Go = -RTlnKeq for us to get the values.

We can see here the folding in the absence of O2 is favorable, as the energy -5.5 Kcal/mol is favoring. The folding pattern with negative Delta G0 is favourable reaction, while a positive  Delta G0 is unfavorable. Generally we have known that if folding is favorable is favorable then the unfolding would be unfavorable and vice-versa.

In this favorable situation the folding of protein with the presence of O2 has to be calculated, this is unfavorable, so the Delta Gfolding would be a positive effect one, in the O2 saturated situation.

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