Why might adding a strong reducing agent like Dithiothreitol (DTT) help denature an extracellular protein? Disulfide bonds might be reduced that might be critical in stabilizing its structure O Disulfide bonds might be oxidized that might be critical in stabilizing its structure Disulfide bonds formed inside the cytoplasm can be oxidized O Cysteines can be reduced to form stabilizing disulfide bonds

Biology Today and Tomorrow without Physiology (MindTap Course List)
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Chapter3: Cell Structure
Section: Chapter Questions
Problem 8SQ: In a lipid bilayer, the of all the lipid molecules are sandwiched between all of the __________. a....
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Why might adding a strong reducing agent like Dithiothreitol
(DTT) help denature an extracellular protein?
O Disulfide bonds might be reduced that might be critical in stabilizing
its structure
O Disulfide bonds might be oxidized that might be critical in stabilizing
its structure
O Disulfide bonds formed inside the cytoplasm can be oxidized
O Cysteines can be reduced to form stabilizing disulfide bonds
Transcribed Image Text:Why might adding a strong reducing agent like Dithiothreitol (DTT) help denature an extracellular protein? O Disulfide bonds might be reduced that might be critical in stabilizing its structure O Disulfide bonds might be oxidized that might be critical in stabilizing its structure O Disulfide bonds formed inside the cytoplasm can be oxidized O Cysteines can be reduced to form stabilizing disulfide bonds
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