Zinc transfer potentials of the alpha - and beta-clusters of metallothionein are affected by domain interactions in the whole molecule.

@article{Jiang2000ZincTP,
  title={Zinc transfer potentials of the alpha - and beta-clusters of metallothionein are affected by domain interactions in the whole molecule.},
  author={Liying Jiang and Milan Va{\vs}{\'a}k and Bert L. Vallee and Wolfgang Maret},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 6},
  pages={2503-8}
}
The alpha- and beta-polypeptides of human metallothionein (isoform 2), obtained by chemical synthesis, were converted into their respective zinc/thiolate clusters, and each domain was investigated separately. Proton titration data for the N-terminal beta-domain fit a simple model with three ionizations of the same apparent pK(a) value of 4.9 and a collective binding constant for zinc of 5 x 10(-12) M at pH 7.0. The zinc cluster in the C-terminal alpha-domain is more stable than that in the beta… CONTINUE READING

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