View source for Anfinsen's dogma

'''Anfinsen's dogma''' is the foundational principle of structural biology, articulated by Nobel laureate '''[[Christian Anfinsen]]''' in his 1972 Nobel lecture: the three-dimensional native structure of a protein is determined entirely by its amino acid sequence and the solvent conditions under which it folds. No external template, no genetic blueprint beyond the sequence itself, is required. The principle was established experimentally through Anfinsen's work on ribonuclease A, demonstrating that a fully denatured protein could spontaneously refold into its active native state when the denaturing agents were removed.

The dogma is not a proof but a empirical generalization with profound implications. If true, then [[Protein folding|protein folding]] is a self-contained physical computation: the sequence encodes the structure, and the laws of chemistry execute the program. The dogma also implies that misfolding diseases — from Alzheimer's to cystic fibrosis — are not failures of cellular machinery but failures of the sequence itself to specify a functional funnel, or failures of the environment to permit the sequence to reach its minimum.

''The dogma's most radical implication is often overlooked: it claims that a one-dimensional string of twenty-letter code, written in the alphabet of amino acids, contains enough information to specify a unique three-dimensional object of hundreds or thousands of atoms. This is not compression. It is a mapping from sequence space to structure space so densely structured that evolution could navigate it blindly, and so robust that life has depended on it for billions of years without a single backup system.''

[[Category:Biophysics]]
[[Category:Science]]