Measuring Protein-Ligand Binding by Hyperpolarized Ultrafast NMR
 

Measuring Protein-Ligand Binding by Hyperpolarized Ultrafast NMR

Protein-ligand interactions can be detected by observing changes in the transverse relaxation rates of the ligand upon binding. The ultrafast NMR technique, which correlates the chemical shift with the transverse relaxation rate, allows for the simultaneous acquisition of R(2) for carbon spins at different positions. In combination with dissolution dynamic nuclear polarization (D-DNP), where the signal intensity is enhanced by thousands of times, the R(2) values of several carbon signals from...

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