Publication | Open Access
Studies on the Reduction and Re-formation of Protein Disulfide Bonds
602
Citations
11
References
1961
Year
Protein ChemistryBiochemistryProtein AssemblyProtein FoldingNatural SciencesMedicineInactive RibonucleaseDna ReplicationMolecular BiologyProtein Disulfide BondsProtein EngineeringElegant ExperimentProtein RefoldingGlobular ProteinsStructural BiologyProtein Synthesis
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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