Protein folding

When the molecular structure of proteins was first studied in the 1950s it was assumed that given their amino acid sequences pure minimization of energy would determine their often elaborate overall shapes. But by the 1990s it was fairly clear that in fact many details of the actual processes by which proteins are assembled can greatly affect their specific pattern of folding. (Examples include effects of chaperone molecules and prions.) (See pages 1003 and 1184.)