Anfinsen's dogma is a postulate in molecular biology championed by the Nobel prize laureate Christian B. Anfinsen. The dogma states that a protein's three dimensional structure is determined only by the protein's amino acid sequence. Implicitly this means that the stable structure of a protein is the lowest energy conformation of a particular sequence. Molecular biology is the study of biology at a molecular level. ... Nobel Prize medal. ... Christian Boehmer Anfinsen, Jr. ... Proteins are amino acid chains, made up from 20 different L-α-amino acids, also referred to as residues, that fold into unique three-dimensional protein structures. ... The general structure of an amino acid molecule, with the amine group on the left and the carboxyl group on the right. ... A protein primary structure is a chain of amino acids. ...

How the protein reaches this structure is the subject of the field of protein folding, that has a related dogma called Levinthal's Paradox. Levinthal's paradox states that the number of possible conformations available to a given protein is astronomically large. Effectively, this make computational prediction of protein structure by evaluating all possible conformations unfeasible even for relatively small proteins. Protein folding is the process by which a protein assumes its characteristic functional shape or tertiary structure, also known as the native state. ...

Also, some proteins need the assistance of another protein called a chaperone to fold properly. It has been suggested that this disproves Anfinsen's dogma. However the chaperones do not appear to affect the final state of the protein, but seems to primarily work by preventing aggregation of several protein molecules before the protein is folded. In biology, chaperones are proteins whose function is to assist other proteins in achieving proper folding. ...