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?

Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
icon
Related questions
Question

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?
Expert Solution
trending now

Trending now

This is a popular solution!

steps

Step by step

Solved in 3 steps with 1 images

Blurred answer
Knowledge Booster
Analytical Separations
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.
Recommended textbooks for you
Chemistry
Chemistry
Chemistry
ISBN:
9781305957404
Author:
Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:
Cengage Learning
Chemistry
Chemistry
Chemistry
ISBN:
9781259911156
Author:
Raymond Chang Dr., Jason Overby Professor
Publisher:
McGraw-Hill Education
Principles of Instrumental Analysis
Principles of Instrumental Analysis
Chemistry
ISBN:
9781305577213
Author:
Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher:
Cengage Learning
Organic Chemistry
Organic Chemistry
Chemistry
ISBN:
9780078021558
Author:
Janice Gorzynski Smith Dr.
Publisher:
McGraw-Hill Education
Chemistry: Principles and Reactions
Chemistry: Principles and Reactions
Chemistry
ISBN:
9781305079373
Author:
William L. Masterton, Cecile N. Hurley
Publisher:
Cengage Learning
Elementary Principles of Chemical Processes, Bind…
Elementary Principles of Chemical Processes, Bind…
Chemistry
ISBN:
9781118431221
Author:
Richard M. Felder, Ronald W. Rousseau, Lisa G. Bullard
Publisher:
WILEY