The folding nucleus of the insulin superfamily: a flexible peptide model foreshadows the native state.

@article{Hua2006TheFN,
  title={The folding nucleus of the insulin superfamily: a flexible peptide model foreshadows the native state.},
  author={Qing-xin Hua and John P. Mayer and Wenhua Jia and Jingwen Zhang and Michael A Weiss},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 38},
  pages={28131-42}
}
Oxidative folding of insulin-like growth factor I (IGF-I) and single-chain insulin analogs proceeds via one- and two-disulfide intermediates. A predominant one-disulfide intermediate in each case contains the canonical A20-B19 disulfide bridge (cystines 18-61 in IGF-I and 19-85 in human proinsulin). Here, we describe a disulfide-linked peptide model of this on-pathway intermediate. One peptide fragment (19 amino acids) spans IGF-I residues 7-25 (canonical positions B8-B26 in the insulin… CONTINUE READING