John, Michael; Headlam, Madeleine; Dixon, Nicholas; Otting, Gottfried
Paramagnetic metal ions in proteins provide a rich source of structural information, but the resonance assignments required to extract the information can be challenging. Here we demonstrate that paramagnetically shifted 15N-HSQC cross-peaks can be assigned using NZ-exchange spectroscopy under conditions in which the paramagnetic form of the protein is in dynamic equilibrium with its diamagnetic form. Even slow exchange of specifically bound metal ions may be detected within the long lifetime...[Show more]
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