Homework Help is Here – Start Your Trial Now!
Science
Biochemistry
Disulfide bonds have been shown to stabilize proteins (i.e., make them less likely to unfold). Consider the cases shown schematically below for two variants of the same protein. In case #1 the disulfide forms between Cys residues that have been introduced near the protein N- and C-termini, and in case # 2 the disulfide forms between Cys residues that have been introduced in the middle of the protein sequence. foof Case #1: Disulfide forms near termini N s-s- Case #2: Disulfide forms in middle of protein ▼ Part A Which protein is likely to be more stable? (Note: Assume the disulfide bond is intact in both the unfolded and folded states). Explain your reasoning. Match the items in the left column to the appropriate blanks in the sentences on the right. folded unfolded #1 # 2 Reset Help Protein will be more stable when folded. This is best explained because its disulfide bond provides a greater degree of conformational constraints on the form as compared to the disulfide bond in protein This means the unfolded form of protein will be less stable than that of leading to a greater protein stability when folded.

Disulfide bonds have been shown to stabilize proteins (i.e., make them less likely to unfold). Consider the cases shown schematically below for two variants of the same protein. In case #1 the disulfide forms between Cys residues that have been introduced near the protein N- and C-termini, and in case # 2 the disulfide forms between Cys residues that have been introduced in the middle of the protein sequence. foof Case #1: Disulfide forms near termini N s-s- Case #2: Disulfide forms in middle of protein ▼ Part A Which protein is likely to be more stable? (Note: Assume the disulfide bond is intact in both the unfolded and folded states). Explain your reasoning. Match the items in the left column to the appropriate blanks in the sentences on the right. folded unfolded #1 # 2 Reset Help Protein will be more stable when folded. This is best explained because its disulfide bond provides a greater degree of conformational constraints on the form as compared to the disulfide bond in protein This means the unfolded form of protein will be less stable than that of leading to a greater protein stability when folded.

Biochemistry
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
See similar textbooks
icon
Related questions
Question

61.12

Disulfide bonds have been shown to stabilize proteins (i.e., make them less likely to unfold). Consider the cases shown schematically below for two variants of the same protein. In case #1 the disulfide forms between Cys residues that have been introduced near the protein N- and C-termini, and in case #2 the disulfide forms between Cys residues that have been introduced in the middle of the protein sequence. N goof Case #1: Disulfide forms near terminl N S-S- Case #2: Disulfide forms in middle of protein Part A Which protein is likely to be more stable? (Note: Assume the disulfide bond is intact in both the unfolded and folded states). Explain your reasoning. Match the items in the left column to the appropriate blanks in the sentences on the right. Submit folded unfolded #1 #2 Previous Answers Reset Protein will be more stable when folded. This is best explained because its disulfide bond provides a greater degree of conformational constraints on the form as compared to the disulfide bond in protein This means the unfolded form of protein will be less stable than that of protein stability when folded. Not completed before the time limit; correct answer displayed Help leading to a greater
Transcribed Image Text:Disulfide bonds have been shown to stabilize proteins (i.e., make them less likely to unfold). Consider the cases shown schematically below for two variants of the same protein. In case #1 the disulfide forms between Cys residues that have been introduced near the protein N- and C-termini, and in case #2 the disulfide forms between Cys residues that have been introduced in the middle of the protein sequence. N goof Case #1: Disulfide forms near terminl N S-S- Case #2: Disulfide forms in middle of protein Part A Which protein is likely to be more stable? (Note: Assume the disulfide bond is intact in both the unfolded and folded states). Explain your reasoning. Match the items in the left column to the appropriate blanks in the sentences on the right. Submit folded unfolded #1 #2 Previous Answers Reset Protein will be more stable when folded. This is best explained because its disulfide bond provides a greater degree of conformational constraints on the form as compared to the disulfide bond in protein This means the unfolded form of protein will be less stable than that of protein stability when folded. Not completed before the time limit; correct answer displayed Help leading to a greater
Expert Solution
trending now

Trending now

This is a popular solution!

steps

Step by step

Solved in 3 steps with 1 images

SEE SOLUTIONCheck out a sample Q&A here
Blurred answer
Similar questions
Recommended textbooks for you
Biochemistry
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
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…
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON
SEE MORE TEXTBOOKS