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Disulfide Interchange and the Three-Dimensional Structure of Proteins

 Digital Record
Identifier: 101584571X168


  • Publication: 1965


9 Pages



This article was published after Anfinsen's laboratory had delineated and demonstrated the major principles of protein folding and during a period when research at the lab turned to the disulfide interchange enzyme that accelerates the reactivation of the reduced form of ribonuclease. In the lab, Givol and Goldberger had worked to achieve in vitro the reactivation rates that would be compatible with the rate of protein biosynthesis. Purifying the enzyme proved difficult, so the team decided to utilize disulfide interchange activity to demonstrate other aspects related to protein folding and structure. The results of these experiments were consistent with the idea that the disulfide bonds in chymtrypsinogen were formed according to the information present in the single-chain protein, which is subsequently converted by peptide bond cleavage to the metastable three-chain chymotrypsin. Based on this, Anfinsen's group reasoned that the inactivation of a multi-chain protein by disulfide interchange indicated its origin as a single-chain protein during biosynthesis.

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Givol, David, Francesco De Lorenzo, Robert Goldberger, and Christian B. Anfinsen. "Disulfide Interchange and the Three-Dimensional Structure of Proteins." Proceedings of the National Academy of Sciences of the United States of America 53, (1965): 676-684. Article. 9 Images.

Proceedings of the National Academy of Sciences of the United States of America

Physical Description

Physical Condition - Poor

Photocopy Only

Collecting Area Details

Part of the Archives and Modern Manuscripts Collection Collecting Area

8600 Rockville Pike
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