Abstract
The formation constants for complexes of Zn(II) with GHL and related peptides have been determined by means of potentiometric titration and 1H NMR spectroscopy in aqueous solution. GHL has a high affinity for Zn(II) but this somewhat higher affinity compared to the related peptides AH, LH and HL is not a sufficient explanation for its biological role. 1H NMR spectroscopy allows structural assignment of the relative chemical shifts to complex structures and the method, therefore, is a powerful tool for the determination of complex structures when the metal ion is diamagnetic and the ESR method previously applied to the GHLCu(II) system (see ref. 4) cannot be used.
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