What is Anfinsen's dogma?
[[Image:RibonucleaseA SS paleRib.png|thumb|right| Folded, 3-D structure of ribonuclease A]] '''Anfinsen's [[dogma]]''' is a [[hypothesis]] in [[molecular biology]] suggested by [[Christian Anfinsen]]. The idea is that a [[protein folding]] into its [[protein structure|native structure]] is done automatically by the protein's [[amino acid]] [[sequence]].<ref>{{cite journal | author=Anfinsen CB | title=Principles that govern the folding of protein chains | journal=Science | volume=181 |issue=4096 |year=1973 | pages=223–230 | pmid=4124164 | doi=10.1126/science.181.4096.223}}</ref> It is only true for some proteins. For other proteins, [[Chaperone (protein)|chaperones]] are needed. Anfinsen shared the 1972 [[Nobel Prize for Chemistry]] for his work on the structure of the [[enzyme]] [[ribonuclease A]].<ref>[http://www.nobelprize.org/nobel_prizes/chemistry/laureates/1972/presentation-speech.html Nobel Prize Award Ceremony speech]</ref><ref>{{cite journal | author=White FH | title=Regeneration of native secondary and tertiary structures by air oxidation of reduced ribonuclease | url=https://archive.org/details/sim_journal-of-biological-chemistry_1961-05_236_5/page/1353 | journal=J. Biol. Chem. | volume=236 |year=1961 | issue=5 | pages=1353–1360 | doi=10.1016/S0021-9258(18)64176-6 | pmid=13784818| doi-access=free }}</ref><ref>{{cite journal | author=Anfinsen CB, Haber E, Sela M, White FH Jr | title=The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain | journal=PNAS | volume=47 | issue=9 |year=1961 | pages=1309–1314 | pmid=13683522 | doi=10.1073/pnas.47.9.1309 | pmc=223141| doi-access=free }}</ref> The dogma suggests that, in the conditions at which folding occurs,<ref>temperature, solvent concentration and composition, etc.</ref> the native structure is a unique and stable state. There are three conditions: ;''uniqueness'': requires that the sequence does not have any other configuration with a comparable [[Gibbs free energy|free energy]]. ;''stability'': small changes in