1D- and 2D-NMR studies of the pH effects on the metal-site geometry in nickel(II)–azurin from Pseudomonas aeruginosa
Abstract
The isotropically shifted proton resonances in nickel(II)–azurin have been assigned on a firm basis by using 1D- and 2D-NMR methods which has allowed the subtle structural changes on the metal binding site associated with the pH induced conformational change in this protein to be revealed.
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