Redox-active bis-cysteinyl peptides. II. Comparative study on the sequence-dependent tendency for disulfide loop formation.

@article{Siedler1994RedoxactiveBP,
  title={Redox-active bis-cysteinyl peptides. II. Comparative study on the sequence-dependent tendency for disulfide loop formation.},
  author={Frank Siedler and Daniela Quarzago and S Rudolph-B{\"o}hner and Luis Moroder},
  journal={Biopolymers},
  year={1994},
  volume={34 11},
  pages={1563-72}
}
Bis(cysteinyl)octapeptides related to the active sites of the oxidoreductases protein disulfide isomerase (PDI), thioredoxin reductase (trr), glutaredoxin (grx), and thioredoxin (trx) were analyzed for their propensity to form the intramolecular 14-membered disulfide ring in oxidation experiments. The rank order of percentage of cyclic monomer formed in aqueous buffer (pH 7.0) at 10(-3) M concentration was found to be very similar, but opposite to that of the Kox and, correspondingly, of the… CONTINUE READING