Differentiation of histidine tautomeric states using 15N selectively filtered 13C solid-state NMR spectroscopy
 

Differentiation of histidine tautomeric states using 15N selectively filtered 13C solid-state NMR spectroscopy

Publication date: Available online 26 June 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Yimin Miao , Timothy A. Cross , Riqiang Fu</br>
The histidine imidazole ring in proteins usually contains a mixture of three possible tautomeric states (two neutral - ? and ? states and a charged state) at physiological pHs. Differentiating the tautomeric states is critical for understanding how the histidine residue participates in many structurally and functionally important proteins. In this work, one dimensional 15N selectively filtered 13C solid-state NMR spectroscopy is proposed to differentiate histidine tautomeric states and to identify all 13C resonances of the individual imidazole rings in a mixture of tautomeric states. When 15N selective 180° pulses are applied to the protonated or non-protonated nitrogen region, the 13C sites that are bonded to the non-protonated or protonated nitrogen sites can be identified, respectively. A sample of 13C,15N labeled histidine powder lyophilized from a solution at pH 6.3 has been used to illustrate the usefulness of this scheme by uniquely assigning resonances of the neutral ? and charged states from the mixture.
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