Homework Help is Here – Start Your Trial Now!
Science
Chemistry
1) Proteins undergo a process called thermal denaturation. This is a process where the protein unfolds (denaturates) as the temperature is increased. (This has important practical consequences for protein based pharmaceuticals). Later this semester we will see that proteins can also denaturate if they are cooled too much. For now we will consider heat denaturation: Protein (folded) → Protein(unfolded) . For a certain protein Adenaturation H is 418.0 k.J mol¬! and Adenaturation S = 1.30 k.J K-1 mol-1. Assume that these values of Adenaturation H and Adenaturation S are independent of temperature (this is actually a bad assumption in real life). A) Calculate AdenaturationG at 310 K. Do you expect the thermal denaturation of the protein to be spontaneous? B) Does the entropy change favor the folded state or the unfolded state at 310 K? C) At what temperature is AdenaturationG zero? We usually call this temperature the “melting temperature" of the protein.

1) Proteins undergo a process called thermal denaturation. This is a process where the protein unfolds (denaturates) as the temperature is increased. (This has important practical consequences for protein based pharmaceuticals). Later this semester we will see that proteins can also denaturate if they are cooled too much. For now we will consider heat denaturation: Protein (folded) → Protein(unfolded) . For a certain protein Adenaturation H is 418.0 k.J mol¬! and Adenaturation S = 1.30 k.J K-1 mol-1. Assume that these values of Adenaturation H and Adenaturation S are independent of temperature (this is actually a bad assumption in real life). A) Calculate AdenaturationG at 310 K. Do you expect the thermal denaturation of the protein to be spontaneous? B) Does the entropy change favor the folded state or the unfolded state at 310 K? C) At what temperature is AdenaturationG zero? We usually call this temperature the “melting temperature" of the protein.

Chemistry
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...
See similar textbooks
icon
Related questions
Question

NOT a graded assignment. From my understanding it is just (Delta G) = (Delta H) - (T)(Delta S) for part A. I am confused about the "unfolding" part and the last part.

1) Proteins undergo a process called thermal denaturation. This is a process where the protein unfolds (denaturates) as the temperature is increased. (This has important practical consequences for protein based pharmaceuticals). Later this semester we will see that proteins can also denaturate if they are cooled too much. For now we will consider heat denaturation: Protein (folded) → Protein(unfolded) . For a certain protein Adenaturation H is 418.0 kJ mol-' and Adenaturation S = 1.30kJ K-1 mol-1. Assume that these values of Adenaturation H and Adenaturation S are independent of temperature (this is actually a bad assumption in real life). A) Calculate AdenaturationG at 310 K. Do you expect the thermal denaturation of the protein to be spontaneous? B) Does the entropy change favor the folded state or the unfolded state at 310 K? C) At what temperature is AdenaturationG zero? We usually call this temperature the "melting temperature" of the protein.
Transcribed Image Text:1) Proteins undergo a process called thermal denaturation. This is a process where the protein unfolds (denaturates) as the temperature is increased. (This has important practical consequences for protein based pharmaceuticals). Later this semester we will see that proteins can also denaturate if they are cooled too much. For now we will consider heat denaturation: Protein (folded) → Protein(unfolded) . For a certain protein Adenaturation H is 418.0 kJ mol-' and Adenaturation S = 1.30kJ K-1 mol-1. Assume that these values of Adenaturation H and Adenaturation S are independent of temperature (this is actually a bad assumption in real life). A) Calculate AdenaturationG at 310 K. Do you expect the thermal denaturation of the protein to be spontaneous? B) Does the entropy change favor the folded state or the unfolded state at 310 K? C) At what temperature is AdenaturationG zero? We usually call this temperature the "melting temperature" of the protein.
Expert Solution
trending now

Trending now

This is a popular solution!

steps

Step by step

Solved in 2 steps with 1 images

SEE SOLUTIONCheck out a sample Q&A here
Blurred answer
Knowledge Booster
Growth and Structure of Solid Surfaces
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
SEE MORE TEXTBOOKS