Inclusion body formation and protein stability in sequence variants of interleukin-1 beta.

@article{Chrunyk1993InclusionBF,
  title={Inclusion body formation and protein stability in sequence variants of interleukin-1 beta.},
  author={Boris A. Chrunyk and John T. Evans and Jay S. Lillquist and Philippe Georges Young and Ronald C. Wetzel},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 24},
  pages={
          18053-61
        }
}
Inclusion body formation during recombinant protein expression in bacteria is of both fundamental interest and practical importance. To elucidate molecular mechanisms of this process, we are examining the in vitro folding and stability properties of a series of human interleukin-1 beta (IL-1 beta) sequence variants which exhibit widely differing tendencies to form inclusion bodies. Of 67 variants surveyed, nine, including wild type, were purified and their in vitro stability properties… CONTINUE READING

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