Table 3.1 in the Biochemistry textbook (Garrett & Grisham) shows the thermodynamic parameters for denaturation of various proteins.
Using the values given, calculate delta Go for myoglobin denaturation at the given pH (9) and temperature(25oC).
Is the unfolding driven by entropy or enthalpy? Explain.
Assuming delta Ho and delta So are invariant with temperature, at what temeparture (oC) will the ratio of [folded myoglobin]/[unfolded myoglobin]=1
How does your calculated value compare to the experimentally determined Tm for myoglobin of about 80oC. What can you conclude from this?