Factors governing selective formation of specific disulfides in synthetic variants of alpha-conotoxin.

@article{Zhang1991FactorsGS,
  title={Factors governing selective formation of specific disulfides in synthetic variants of alpha-conotoxin.},
  author={Rongguang Zhang and George H. Snyder},
  journal={Biochemistry},
  year={1991},
  volume={30 47},
  pages={11343-8}
}
alpha-Conotoxin GI is a snail toxin protein consisting of 13 amino acids cross-linked by 2 intramolecular disulfide bridges. This toxin is an antagonist of acetylcholine receptors. The native sequence has been synthesized, along with nine additional variants in which non-cysteine residues are replaced by alanine or the cysteine positions are altered. Each reduced peptide has been oxidized by reaction with oxygen or glutathione both in a folding buffer and in 6 M guanidine hydrochloride… CONTINUE READING