Role of lysine side chains in metallothionein |
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Authors: | M Vašák Ch E McClelland H A O Hill J H R Kägi |
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Institution: | (1) Biochemisches Institut der Universität Zürich, CH-8057 Zürich, Switzerland;(2) Inorganic Chemistry Laboratory, OX1 3QR Oxford, England |
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Abstract: | Summary pKa-Values of lysine residues of mammalian metallothionein were determined by chemical titration measurements of -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.To whom correspondence concerning this paper should be addressed. |
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Keywords: | Metallothionein 1H-NMR circular dichroism electrostatic interactions lysine residues pH-titration |
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