Question

n the 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?

Answer 1

Answer and Explanation:

The regular synthetic denaturant of proteins is urea. The high grouping of urea causes unfolding of protein and accordingly brings about loss of capacity of protein. The urea communicates with the protein and counteracts collapsing of protein.

During oxidation, the disufide bonds that are required for legitimate working and adjustment of protein are shaped, while in nearness of urea, the disulfide bonds are not situated effectively. The protein oxidation brings about covalent adjustment of protein that outcomes in change of physical and substance properties of protein.

The difference in physical and chemical properties of protein after oxidation and in nearness of urea can't be altered even after expulsion of urea. Along these lines, protein doesn't crease appropriately.