ABSTRACT
The biochemical function of a protein is determined largely by its threedimensional structure. In turn, the structure of a protein is mainly dictated by the specific linear sequence of its amino acids, as first demonstrated by Anfinsen in a historical experiment. He showed that a protein (in that particular case, ribonuclease A) once denatured-that is, unfolded-
in vitro
recovers its “native” conformation when the denaturing agents are removed from the test tube. The same experiment can be conducted with a chemically synthesized protein, which implies that the information about the threedimensional structure of a protein is contained in its amino acid sequence. Subsequently, cellular mechanisms were discovered that catalyze folding of some proteins. These systems accelerate the folding process, but do not affect the structure of the final native state.
