Probing the disulfide folding pathway of insulin-like growth factor-I.

@article{Milner1999ProbingTD,
  title={Probing the disulfide folding pathway of insulin-like growth factor-I.},
  author={Steven J Milner and John A Carver and F. John Ballard and Geoffrey Leonard Francis},
  journal={Biotechnology and bioengineering},
  year={1999},
  volume={62 6},
  pages={
          693-703
        }
}
The crucial step of folding of recombinant proteins presents serious challenges to obtaining the native structure. This problem is exemplified by insulin-like growth factor (IGF)-I which when refolded in vitro produces the native three-disulfide structure, an alternative structure with mispaired disulfide bonds and other isomeric forms. To investigate this phenomenon we have examined the refolding properties of an analog of IGF-I which contains a 13-amino acid N-terminal extension and a charge… CONTINUE READING