Why reversing the sequence of the alpha domain of human metallothionein-2 does not change its metal-binding and folding characteristics.

@article{Pan1999WhyRT,
  title={Why reversing the sequence of the alpha domain of human metallothionein-2 does not change its metal-binding and folding characteristics.},
  author={Peng-min Pan and Zhan Feng Zheng and Ping Chiang Lyu and Philip C. Huang},
  journal={European journal of biochemistry},
  year={1999},
  volume={266 1},
  pages={33-9}
}
A novel peptide, the backward reading sequence of human metallothionein-2 alpha domain, was synthesized and its chemical and spectroscopic properties analyzed. This folded retro-alpha domain was able to bind Cd(II) in identical stoichiometries with the chemically synthesized alpha domain of metallothionein-2. Nearly identical to the alpha domain, Cd-binding retro-alpha domain showed a characteristic ultraviolet absorption spectrum with a shoulder at 245-250 nm (due to cadmium-thiolate charge… CONTINUE READING

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