Acidic residues on the N-terminus of proinsulin C-Peptide are important for the folding of insulin precursor.

@article{Chen2002AcidicRO,
  title={Acidic residues on the N-terminus of proinsulin C-Peptide are important for the folding of insulin precursor.},
  author={Li-ming Chen and X Yang and J Tang},
  journal={Journal of biochemistry},
  year={2002},
  volume={131 6},
  pages={855-9}
}
To investigate the role of C-peptide in the folding of insulin precursor, a series of C-peptide mutant proinsulin genes were constructed, overexpressed in Escherichia coli and the proteins purified. Correct disulfide linkages of these proteins were confirmed by both tryptic peptide mapping and insulin receptor binding analyses. In vitro refolding experiments were performed with the purified proteins and showed that mutations on the glycine-rich middle segment of C-peptide, GGGPGAG, and deletion… CONTINUE READING