How does the primary structure of a protein influence its tertiary structure as demonstrated by the Anfinsen Experiment?

What happens to ribonuclease A when both urea and beta mercaptoethanol are added, and what is the outcome when they are removed?

What thermodynamic property of protein folding was demonstrated by the Anfinsen Experiment?

Which protein was used in the Anfinsen Experiment to demonstrate protein folding?

What is the effect of removing only beta mercaptoethanol while keeping urea in the Anfinsen Experiment?

How does the catalytic activity of scrambled proteins compare to normal proteins?

How did Anfinsen's findings impact the field of biochemistry?