The major difference between a protein molecule in its native state and in its denatured state lies in the number of conformations available. To a first approximation, the native, folded state can be thought to have one conformation. The unfolded state can be estimated to have three possible orientations about each bond between residues. Part A For a protein of 150 residues, estimate the entropy change per mole upon denaturation. Express your answer with the appropriate units. AS = μA Value Units heview Constants | Periodic ?
The major difference between a protein molecule in its native state and in its denatured state lies in the number of conformations available. To a first approximation, the native, folded state can be thought to have one conformation. The unfolded state can be estimated to have three possible orientations about each bond between residues. Part A For a protein of 150 residues, estimate the entropy change per mole upon denaturation. Express your answer with the appropriate units. AS = μA Value Units heview Constants | Periodic ?
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
Related questions
Question
3-2.10
Transcribed Image Text:The major difference between a protein molecule in
its native state and in its denatured state lies in the
number of conformations available. To a first
approximation, the native, folded state can be
thought to have one conformation. The unfolded
state can be estimated to have three possible
orientations about each bond between residues.
Part A
For a protein of 150 residues, estimate the entropy change per mole upon denaturation.
Express your answer with the appropriate units.
AS =
Submit
μĂ
Value
Request Answer
Units
Review | Constants | Periodic Table
?
Expert Solution
Step 1: Total number of possible orientations in the protein molecule
The protein molecule is 150 residues long. So, there is 149 peptide bonds. It has been said that, in the denatured state, there are 3 possible orientations per peptide bond.
So, total number of possible orientations per denatured protein molecule is 3149.
Step by step
Solved in 3 steps with 6 images
Recommended textbooks for you
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON