The formation of protein disulphide bonds.
The past year has provided more detail on the formation of native disulphide bonds during protein folding at biosynthesis and has identified important cellular factors in the oxidative folding compartments, namely the eukaryotic endoplasmic reticulum and the bacterial periplasm. This information has enabled traditional in vitro refolding studies to be re-evaluated and their relevance as models for folding in the cell to be established.
Freedman
R B
RB
Research School of Biosciences, Biological Laboratory, University of Kent, Canterbury, UK.
D000818:Animals; D003545:Cysteine / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry*; D006801:Humans; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D004220:Disulfides; D011506:Proteins; D003545:Cysteine