Studies on the Reduction and Re-formation of Protein Disulfide Bonds
- Contributor(s):
- Anfinsen, Christian B. (Christian Boehmer), 1916-1995 Haber, Edgar, 1932-1997 Journal of Biological Chemistry
- Publication:
- American Society for Biochemistry and Molecular Biology, May 1961
- Language(s):
- English
- Format:
- Text
- Subject(s):
- Oxidation-Reduction Ribonucleases Protein Conformation
- Genre(s):
- Archival Materials Articles
- Abstract:
- 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.
- Copyright:
- This item may be under copyright protection; contact the copyright owner for permission before re-use.
- Extent:
- 3 pages
- NLM Unique ID:
- 101584571X142 (See in Profiles in Science)
- Profiles in Science ID:
- KKBBJV
- Permanent Link:
- http://resource.nlm.nih.gov/101584571X142
- Archival Collection:
- The Christian B. Anfinsen Papers (Profiles in Science)