Anfinsenin

Anfinsen's principle, named after Christian B. Anfinsen, is a foundational concept in biochemistry that states the information required for a protein to fold into its native three-dimensional structure is contained in its amino acid sequence. In classic experiments, Anfinsen demonstrated that bovine pancreatic ribonuclease A could be fully denatured and then, once the denaturing conditions were removed, refolded spontaneously into its active form. This showed that the native conformation of a protein could be determined by its sequence alone under appropriate conditions.

The results from these studies led to what is often called the protein folding dogma: the native structure of a protein is determined by its primary sequence, and the information required for folding is embedded in that sequence. This idea helped shape the field of protein biochemistry and the broader understanding of how structure and function relate in biomolecules. Anfinsen was awarded the Nobel Prize in Chemistry in 1972 for his work on ribonuclease and for elucidating the principles governing protein folding.

Subsequent research has refined the view, recognizing that in living cells the folding process is assisted by molecular chaperones and influenced by the cellular environment. While the sequence contains crucial information, folding pathways, misfolding, and aggregation are affected by factors beyond the primary structure. Anfinsen’s work remains a cornerstone of protein science, informing both experimental approaches and theoretical models of how proteins attain their functional forms.