Ask Question
Yesterday, 19:32

When a protein is treated with a reducing agent such as 2-mercaptoethanol it becomes denatured. The interactions stabilizing the protein that are most affected and lead to denaturation with reducing agent treatment are

+2
Answers (1)
  1. Yesterday, 19:43
    0
    Disulfide linkage/bond

    Explanation:

    The tertiary and quarternary structure of the protein is stabilized by Disulfide linkage which is formed between two thiol groups in the protein. 2-mercaptoethanol is a reducing agent that breaks this disulfide bond.

    A protein becomes denature when it loses its native configuration and becomes inactive. So as 2-mercaptoethanol breaks disulfide bond in protein it looses its native configuration and becomes denatured. 2-mercaptoethanol is used in SDS-PAGE to separate protein subunits. Therefore the correct answer is Disulfide linkage/bond.
Know the Answer?
Not Sure About the Answer?
Find an answer to your question 👍 “When a protein is treated with a reducing agent such as 2-mercaptoethanol it becomes denatured. The interactions stabilizing the protein ...” in 📗 Biology if the answers seem to be not correct or there’s no answer. Try a smart search to find answers to similar questions.
Search for Other Answers