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Home Q & A Board Biology-Related Homework Help General Biology
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ilanasw ilanasw
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6 years ago
An artificial myoglobin our lab recently designed has two independent O2 binding sites. The experimentally observed Kd for the first site was 600 nM.

(a) Estimate the observed Kd for the second.
(b) The ΔGfolding for the protein in the absence of O2 is -5.5 kcal/mol. Assuming the unfolded protein cannot bind O2, what is the ΔGfolding in O2 – saturated solution (2 mM)?
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bolbolbolbol
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6 years ago
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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  ΔGo = -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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wrote...
#2
3 years ago Edited: 3 years ago, Tarek munawar
T
wrote...
#3
3 years ago
Thank you!
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