when a protein is treated with 6 m urea it becomes denatured. the interactions stabilizing the protein that is affected and lead to denaturation with urea treatment are hydrogen bonds.
Denaturation of protein results from treating it with urea at a concentration of 6 M. When a protein's typical structure is warped as a result of some of the hydrogen bonds being broken, the protein is said to have become denatured. Because of this, every interaction that is normally present in the protein is disrupted, which ultimately leads to the protein becoming denatured. So hydrogen bonding is the answer to the question.
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