Christian B. Anfinsen Created 2026-10-24 Updated 2026-11-05
Christian B. Anfinsen investigated the relation between amino-acid sequence and protein folding. Refolding experiments connect recovery of a protein's native structure with recovery of its biological activity.
The work supports the thermodynamic interpretation of folding under appropriate conditions: sequence and environment constrain the accessible stable structure. It does not imply that every protein folds rapidly or independently of cellular assistance.[ref]
Figure 1. . Edward A. Hubbard / National Institutes of Health, circa 1950s; courtesy NIH Record and NIH, via the National Library of Medicine. Public domain (PD-USGov-NIH). Source.
Primary paper: Principles that govern the folding of protein chains, Science 181, 223–230 (1973). pubmed.ncbi.nlm.nih.gov/4124164/
Cited passage: thermodynamic hypothesis and reversible refolding experiments under specified environmental conditions.