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Role of lysine side chains in metallothionein (1985)

Vašák, M. ; McClelland, Ch E. ; Hill, H. A. O. ; [et al.]

Springer

Cellular and molecular life sciences 41 (1985), S. 30-34

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ISSN: 1420-9071

Keywords: Metallothionein ; 1H-NMR, circular dichroism ; electrostatic interactions ; lysine residues ; pH-titration

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF02005857

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