In the 1950s, Christian Anfinsen demonstrated the renaturation of the protein ribonuclease (RNase) in vitro. After reduction and the addition of urea, the protein was in an unfolded state. After removing the urea and then the reducing agent, the protein oxidized and refolded, with greater than 90% activity. If reducing agent removal occurs before removing the urea, the protein showed less than 5% activity. Why does RNase refold incorrectly if the reducing agent is removed before urea removal? Contaminants in the RNase preparation would form covalent bonds with the protein, preventing reactivation. Urea would participate in weak bonding interactions with RNase, preventing oxidation of cysteine. Disulfide bonds are not positioned correctly unless weak bonding interactions are present. The protein would not fully denature.
In the 1950s, Christian Anfinsen demonstrated the renaturation of the protein ribonuclease (RNase) in vitro. After reduction and the addition of urea, the protein was in an unfolded state. After removing the urea and then the reducing agent, the protein oxidized and refolded, with greater than 90% activity. If reducing agent removal occurs before removing the urea, the protein showed less than 5% activity. Why does RNase refold incorrectly if the reducing agent is removed before urea removal? Contaminants in the RNase preparation would form covalent bonds with the protein, preventing reactivation. Urea would participate in weak bonding interactions with RNase, preventing oxidation of cysteine. Disulfide bonds are not positioned correctly unless weak bonding interactions are present. The protein would not fully denature.
Human Heredity: Principles and Issues (MindTap Course List)
11th Edition
ISBN:9781305251052
Author:Michael Cummings
Publisher:Michael Cummings
Chapter10: From Proteins To Phenotypes
Section: Chapter Questions
Problem 10QP: b. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein...
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Transcribed Image Text:In the 1950s, Christian Anfinsen demonstrated the renaturation of the protein ribonuclease (RNase) in vitro.
After reduction and the addition of urea, the protein was in an unfolded state. After removing the urea and then the reducing
agent, the protein oxidized and refolded, with greater than 90% activity. If reducing agent removal occurs before removing the
urea, the protein showed less than 5% activity.
Why does RNase refold incorrectly if the reducing agent is removed before urea removal?
Contaminants in the RNase preparation would form covalent bonds with the protein, preventing reactivation.
Urea would participate in weak bonding interactions with RNase, preventing oxidation of cysteine.
Disulfide bonds are not positioned correctly unless weak bonding interactions are present.
The protein would not fully denature.
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