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]
Principles that govern the folding of protein chains by Christian B. Anfinsen. Primary publication: scientific topic and stated experimental result
Biochemist whose research addressed protein folding.[ref]
https://www.nobelprize.org/nomination/archive/show_people.php?id=16045. Primary identity record
Portrait of Christian B. Anfinsen
. 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. Principles that govern the folding of protein chains by Christian B. Anfinsen Created 2026-10-24 Updated 2026-10-31
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.
