Question

Complete the description of Christian Anfinsen's ribonuclease A renaturation experiment. Anfinsen started with purified ribonuclease A in its native state. To begin, he This process resulted in denatured ribonuclease A protein. Next, he which allowed ribonuclease A to return to its native state.

Answer 1

In Anfinsen's ribonuclease A renaturation experiment,he wanted to show that protein folding entirely resides within the amino acid sequence of protein.

Step-by-step explanation:

He used ribonuclease A as a model and removed urea and 2ME from the folding solution.Under these condition, ribonuclease A regains it's biological activity.

This refolding occur in in vitro conditions.

This experiment discover an enzyme called protein disulfide isomerase(PDI) which catalyze the reduction of incorrect dissulfide bonds.This also helps in trapping protein in an incorrect conformationso that it can un fold and try agin.

This PDI plays important role in proper folding,and the active site of this enzyme have disulfide.