Which of the following statements are correct about protein folding (select all that appy)? A. Protein folding is a very slow process with most proteins requiring >30 min to go from unfolded to native conformation B. The mature two-chain form of insulin spontaneously folds into the native conformation C. A sharp transition in the presence of denaturants (See Figue 8.1) suggests the protein folds without intermediates D. Proteins randomly sample each possible conformation before arriving final native state E. Proteins with disulfide bridges tend not follow a simple two-state folding mechanism.
Which of the following statements are correct about protein folding (select all that appy)? A. Protein folding is a very slow process with most proteins requiring >30 min to go from unfolded to native conformation B. The mature two-chain form of insulin spontaneously folds into the native conformation C. A sharp transition in the presence of denaturants (See Figue 8.1) suggests the protein folds without intermediates D. Proteins randomly sample each possible conformation before arriving final native state E. Proteins with disulfide bridges tend not follow a simple two-state folding mechanism.
Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Chapter4: Cells
Section: Chapter Questions
Problem 1ITD
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Question
Which of the following statements are correct about protein folding (select all that appy)?
A. |
Protein folding is a very slow process with most proteins requiring >30 min to go from unfolded to native conformation |
|
B. |
The mature two-chain form of insulin spontaneously folds into the native conformation |
|
C. |
A sharp transition in the presence of denaturants (See Figue 8.1) suggests the protein folds without intermediates |
|
D. |
Proteins randomly sample each possible conformation before arriving final native state |
|
E. |
Proteins with disulfide bridges tend not follow a simple two-state folding mechanism. |
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