Oxidative folding: recent developments

Abstract: Disulfide bond formation in proteins is an effective tool of both structure stabilization and redox regulation. The prokaryotic periplasm and the endoplasmic reticulum of eukaryotes were long considered as the only compartments for enzyme mediated formation of stable disulfide bonds. Recently, the mitochondrial intermembrane space has emerged as the third protein-oxidizing compartment. The classic view on the mechanism of oxidative folding in the endoplasmic reticulum has also been reshaped by new observations. Moreover, besides the structure stabilizing function, reversible disulfide bridge formation in some proteins of the endoplasmic reticulum, seems to play a regulatory role. This review briefly summarizes the present knowledge of the redox systems supporting oxidative folding, emphasizing recent developments.

Object Details

• Location: Deutsche Nationalbibliothek Frankfurt am Main
• Extent: Online-Ressource
• Language: Englisch

References and Relationships

• Bibliographic citation: Oxidative folding: recent developments ; volume:2 ; number:5 ; year:2011 ; pages:379-390 ; Biomolecular concepts ; 2, Heft 5 (2011), 379-390

Contributors, Places and Time

• Creator: Szarka, András ; Bánhegyi, Gábor

Further information

• DOI: 10.1515/BMC.2011.038
• URN: urn:nbn:de:101:1-2409241608221.265815272970
• Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Last update: 15.08.2025, 7:27 AM CEST