Professor Mary Gold wanted to test her hypothesis that the disulfide bridges that form in many proteins do so after the minimum energy conformation of the protein has been achieved. She treated a sample of lysozyme, an enzyme containing four disulfide bridges, with 2-mercaptoethanol and then added urea to denature the enzyme. She slowly removed these reagents so that the enzyme could refold and reform the disulfide bridges. The lysozyme she 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 Professor Gold's hypothesis?