AnfinsenDogma
Anfinsen's dogma, also known as the thermodynamic hypothesis of protein folding, is a principle in biochemistry stating that the native three-dimensional structure of a protein is determined by its amino acid sequence and that, under physiological conditions, the information required to fold into this structure is contained in the sequence alone. The native state is considered the thermodynamically favored conformation, i.e., the global free-energy minimum, assuming a suitable cellular environment.
The concept emerged from Christian B. Anfinsen's experiments in the 1950s and 1960s, which culminated in the
In his classic ribonuclease A experiments, the enzyme was denatured with urea and beta-mercaptoethanol, which reduced
Modern understanding acknowledges that while the amino acid sequence contains the information required for folding, the