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

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)