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- W158768081 abstract "Publisher Summary This chapter deals with folding catalysts, in particular with catalysts that are essential for disulfide bond formation in Escherichia coli. Nevertheless, some of these catalysts contain chaperone activity, demonstrating that these two activities are sometimes found within the same protein molecule. The folding of proteins into their three-dimensional structure is essential for their biological function. For proteins that contain disulfide bonds, formation of these bonds is often an important step in the folding reaction. DsbA is identified by the use of a disulfide indicator protein, MalF-fi-galactosidase. This fusion protein lacks fl-galactosidase activity when present in a wild-type E. coli background that is competent in forming disulfides. Despite their common structures, thioredoxin and DsbA fulfill different functions and exist in different cellular compartments. While thioredoxin acts as a reductant of disulfide bonds in the cytosol introduces disulfide bonds into newly synthesized proteins during their translocation to the periplasm. The small equilibrium constant of DsbA with glutathione demonstrates that the disulfide bond formed by DsbA is highly unstable. The stability of a particular disulfide bond corresponds to the extent to which a protein is stabilized by this bond. In other words, the more stable the disulfide bond, the more stable the protein conformation." @default.
- W158768081 created "2016-06-24" @default.
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- W158768081 date "2001-01-01" @default.
- W158768081 modified "2023-09-25" @default.
- W158768081 title "Catalysis of disulfide bond formation and isomerization in Escherichia coli" @default.
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- W158768081 doi "https://doi.org/10.1016/s0065-3233(01)59009-9" @default.
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