Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.

@article{Gordon1994SelectiveIV,
  title={Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.},
  author={Carl L. Gordon and S K Sather and Sherwood R. Casjens and Jonathan King},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 45},
  pages={27941-51}
}
The in vivo conformational substrates of the GroE chaperonins have been difficult to identify, in part because of limited information on in vivo polypeptide chain folding pathways. Temperature-sensitive folding (tsf) mutants have been characterized for the coat protein and tailspike protein of phage P22. These mutations block intracellular folding at restrictive temperature by increasing the lability of folding intermediates without impairing the stability or function of the native state… CONTINUE READING

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