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Role of lysine side chains in metallothionein

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Summary

pKa-Values of lysine residues of mammalian metallothionein were determined by chemical titration measurements of ɛ-CH2 lysine resonances in the1H-NMR spectra. They are about 0.5 pH-unit higher than the average pKa-value of a metal-free derivative, suggesting interaction of the positively charged residues with the two three-fold negatively charged metal-thiolate clusters of the metal-containing form. Deprotonation of the lysines leads to circular dichroism changes attributable to an electrostatically induced structural transition of the protein.

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Abbreviations

CD:

circular dichroism

DSS:

2,2-dimethyl-2-silapentane-5-sulphonate

TNBS:

2,4,6-trinitrobenzene sulfonic acid

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Authors and Affiliations

  1. Biochemisches Institut der Universität Zürich, CH-8057, Zürich, Switzerland

    M. Vašák & J. H. R. Kägi

  2. Inorganic Chemistry Laboratory, OX1 3QR, Oxford, England

    Ch E. McClelland & H. A. O. Hill

Authors
  1. M. Vašák
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  2. Ch E. McClelland
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  3. H. A. O. Hill
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  4. J. H. R. Kägi
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Vašák, M., McClelland, C.E., Hill, H.A.O. et al. Role of lysine side chains in metallothionein. Experientia 41, 30–34 (1985). https://doi.org/10.1007/BF02005857

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