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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 synthetically produced RNase refold incorrectly if the reducing agent is removed before urea removal?
a: Urea would participate in weak bonding interactions with RNase, preventing oxidation of Cys.
b: Disulfide bonds are not positioned correctly unless weak bonding interactions are present.
c: Contaminants in the RNase preparation would form covalent bonds with the protein, preventing reactivation.
d: The protein would not fully denature.
Answer B.Disulfide bonds are not positioned correctly unless weak bonding interactions are present. Beacause poor bonding interaction properly place the -SH residues to form disulfide bridges when removing the reducing agent (allowing oxidation) when removing the urea. before the removal of urea, oxydation occurs so the cysteine residues may not be located correctly and the disulfide bridges that form in the wrong places resulting in inactive protein.
Answer this question In the 1950s, Christian Anfinsen demonstrated the renaturation of the protein ribonuclease (RNase)...
In the 1950s, Christian Anfinsen demonstrated the renaturation of the protein ribonuclease (RNase) in vitro. After reduction (to reduce the disulfide links) and the addition of urea (to denature the protein), the protein was in an unfolded state. After removing the urea and the reducing agent, the protein refolded, with greater than 90% activity. If the urea were removed after oxidation occurred, the protein had less than 5% activity. Why would the protein not refold correctly if the urea were...