d. Calculate the Gibbs energy and the equilibrium constant for the denaturation of chymotrypsin at pH=2 ant T=310 K. Is the protein stable under these conditions?

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Only answer Part D please 

The denaturation of a biological macromolecule may be described as an equilibrium:
Protein
Denatured
a. Show that the fraction of denatured macromolecules, 0, is related to the equilibrium
constant, Kd, by
K.
1+ Kd
b. At pH=2, the standard enthalpy and entropy of formation for the denaturation of the
enzyme chymotrypsin are 418 kJ/mol and 1.32 kJ K-' mol-', respectively. Use these data
to generate a plot that shows the temperature dependence of 0. Assume the enthalpy and
entropy change to be independent of temperature.
c. The "melting temperature" of a biological molecule is defined as the temperature at
which 0=1/2. Determine the “melting temperature" of chymotrypsin at pH=2.
d. Calculate the Gibbs energy and the equilibrium constant for the denaturation of
chymotrypsin at pH=2 ant T=310 K. Is the protein stable under these conditions?
Transcribed Image Text:The denaturation of a biological macromolecule may be described as an equilibrium: Protein Denatured a. Show that the fraction of denatured macromolecules, 0, is related to the equilibrium constant, Kd, by K. 1+ Kd b. At pH=2, the standard enthalpy and entropy of formation for the denaturation of the enzyme chymotrypsin are 418 kJ/mol and 1.32 kJ K-' mol-', respectively. Use these data to generate a plot that shows the temperature dependence of 0. Assume the enthalpy and entropy change to be independent of temperature. c. The "melting temperature" of a biological molecule is defined as the temperature at which 0=1/2. Determine the “melting temperature" of chymotrypsin at pH=2. d. Calculate the Gibbs energy and the equilibrium constant for the denaturation of chymotrypsin at pH=2 ant T=310 K. Is the protein stable under these conditions?
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