Journal of Biological Chemistry · 1961 · 603 citations · 11 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein BiochemistryProtein FoldingDisulfide Bond FormationGlobular ProteinsProtein DenaturationProtein Folding PathwaysProtein RefoldingProtein StructureAmino Acid Sequence EffectsAmino Acid Sequence-structure RelationshipsDisulfide Bond AnalysisDisulfide Bond ChemistryDisulfide Bond RearrangementEnzyme RefoldingProtein Folding AnalysisProtein Folding Of Enzymes
The information contained in the amino acid sequence of a protein is linear, such as it is in DNA, but proteins function by virtue of the arrangement of their linear structure into a well-defined three-dimensional conformation. In this article, Anfinsen and Haber sought to determine how the two-dimensional data of DNA were translated into the three-dimensional information that was characteristic of globular proteins. This simple and elegant experiment was designed to determine what would happen when reduced, unfolded, and enzymatically inactive ribonuclease was allowed simply to refold in the presence of only neutral aqueous buffer and air. They found that most of the activity of the enzyme was regained.
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Gel filtration of proteins, peptides and amino acids
Jerker Porath · Biochimica et Biophysica Acta · 1960 · 358 citations