Final answer:
Christian Anfinsen's classic experiment showed that the primary structure of ribonuclease A contains all the necessary information for the protein to fold into its native, functional conformation.
Step-by-step explanation:
Christian Anfinsen's ribonuclease A renaturation experiment involved the denaturation and subsequent refolding of the ribonuclease A enzyme, revealing that the primary amino acid sequence contains all the information required for protein folding into its native structure. The renaturation kinetic protocol mentioned in the question pertains to DNA and not directly to Anfinsen's work, but Anfinsen's research does connect to studies on nucleic acids and their role in protein synthesis, as well as the effects of inhibitors on enzymatic activity. In his experiment, ribonuclease A was initially denatured by exposing it to urea and mercaptoethanol, which disrupt the protein's structure. Removing these agents allowed the protein to refold and regain its enzymatic function.
This experiment demonstrated that protein folding is a spontaneous process, guided by the protein's own sequence, which was pivotal in the understanding of protein structure-function relationship.