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
Permalink