Chapter 17, Problem 56P

A chemist wanted to test his hypothesis that the disulfide bridges that form in many proteins do so after the minimum energy conformation of the protein has been achieved. He reduced a sample of an enzyme that contained four disulfide bridges and then added urea to denature the enzyme. He slowly removed these reagents so that the enzyme could re-fold and re-form the disulfide bridges. The enzyme he recovered had 80% of its original activity. What would be the percent activity in the recovered enzyme if disulfide bridge formation were entirely random rather than determined by the tertiary structure? Does this experiment support his hypothesis?