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Dr. Christian B. Anfinsen (formerly with the National Institute of Arthritis, Metabolism, and Digestive Diseases) won the Nobel Prize in Chemistry for his work "on ribonuclease, especially concerning the connection between the amino acid sequence and the biologically active conformation." Dr. Anfinsen provided the first clue to the structure of ribonuclease by demonstrating that it is comprised of a single polypeptide chain. He and his colleagues at Rockefeller University (with whom he shared the prize) demonstrated that the information required to fold the polypeptide chain of ribonuclease into the specific three-dimensional form of the active enzyme resides in the sequence of amino acids. Therefore, it became clear that this protein could be synthesized in the laboratory by joining the proper amino acids in the correct order and then allowing the chain of amino acids to fold spontaneously. This led to the first synthesis of an enzyme from chemicals in the laboratory. Such studies are basic to an understanding of normal life processes as well as of inherited metabolic diseases.