Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein

@article{Robinson1997DisulphidebondedIO,
  title={Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein},
  author={Anne S. Robinson and Jonathan King},
  journal={Nature Structural Biology},
  year={1997},
  volume={4},
  pages={450-455}
}
The trimeric parallel β-coil P22 tailspike contains eight cysteines per chain, but lacks disulphide bonds in the native state, in both the crystalline and solution forms. However, cysteines in a folding intermediate are reactive with thiol blocking reagents, which prevent further productive folding both in vivo and in vitro. The in vivo refolding yield was independent of the availability of metal ions, but was sensitive to redox potential. Isolation by nondenaturing gel electrophoresis of the… CONTINUE READING
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