Nthe 1950’s, anfinsen carried out denaturation and renaturation experiments of the protein rnase (ribonuclease) in vitro. after using -mercaptoethanol to reduce the disulfide links and urea to denature the protein, the protein was in an unfolded, or denatured, 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. which is the best explanation for why the protein would not refold correctly if the urea were removed after the reducing agent was removed?
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Nthe 1950’s, anfinsen carried out denaturation and renaturation experiments of the protein rnase (ri...
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