Title:

Studies on the Reduction and Re-formation of Protein Disulfide Bonds

Creator:

Anfinsen, Christian B. (Christian Boehmer), 1916-1995
Haber, Edgar, 1932-1997

Date:

May 1961

Description:

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.

Periodical:

Journal of Biological Chemistry

Publisher:

American Society for Biochemistry and Molecular Biology

Location:

Box: 27. Folder: 5

Rights:

Reproduced with permission of the American Society for Biochemistry and Molecular Biology. and http://www.jbc.org/

Genre:

Articles

Subject:

Oxidation-Reduction, Ribonucleases, and Protein Conformation

Format:

Text

Extent:

3 pages

Language:

English

Legacy Source Citation:

Periodical. Anfinsen, Christian B., and Edgar Haber. "Studies on the Reduction and Re-formation of Protein Disulfide Bonds." Journal of Biological Chemistry 236, 5 (May 1961): 1361-1363. Article. 3 Images.. Journal of Biological Chemistry

Legacy ID:

KKBBJV

NLM ID:

101584571X142

Profiles Collection:

The Christian B. Anfinsen Papers

Shareable Link:

https://profiles.nlm.nih.gov/101584571X142

Story Section:

Protein Folding and the Thermodynamic Hypothesis, 1950-1962