Increasing the reactivity of an artificial dithiol-disulfide pair through modification of the electrostatic milieu.

@article{Hansen2005IncreasingTR,
  title={Increasing the reactivity of an artificial dithiol-disulfide pair through modification of the electrostatic milieu.},
  author={Rosa E Hansen and Henrik {\O}stergaard and Jakob R Winther},
  journal={Biochemistry},
  year={2005},
  volume={44 15},
  pages={
          5899-906
        }
}
The thiol-disulfide exchange reaction plays a central role in the formation of disulfide bonds in newly synthesized proteins and is involved in many aspects of cellular metabolism. Because the thiolate form of the cysteine residue is the key reactive species, its electrostatic milieu is thought to play a key role in determining the rates of thiol disulfide exchange reactions. While modest reactivity effects have previously been seen in peptide model studies, here, we show that introduction of… CONTINUE READING

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