Single-Scan Characterization of ¹⁴N Nuclei via ¹H-Detected Rotating-Frame Relaxometry

$^{14}$N NMR is notoriously difficult to perform in liquids due to the very fast spin relaxation and the large quadrupolar couplings, which render many signals invisible. We show here how $^{14}$N nuclei of biomolecular constituents can be probed indirectly by reintroducing the scalar relaxation of the second kind contribution to the polarization lifetimes of J-coupled protons in double resonance spin-locking experiments. The enhanced $^1$H relaxation rates in the rotating-frame allow for direct evaluation of nitrogen chemical shift and polarization lifetimes, from which one- and even two-bond $^1$H-$^{14}$N scalar couplings as well as $^{14}$N quadrupolar interactions can be determined. We demonstrate the versatility of this method by characterizing $^1$H-$^{14}$N spin pairs in several molecules of biological importance, showing proton relaxation enhancements beyond one order of magnitude. We further observe a pronounced effect from intermolecular hydrogen bonding. Our approach can be readily integrated into existing biomolecular NMR methodologies, as demonstrated here for $^1$H-detected relaxation-editing experiments with water suppression. This method provides access to nitrogen's picosecond-modulated quadrupolar interaction via single-scan proton detection in systems that would otherwise yield almost no detectable direct $^{14}$N signal even after averaging over thousands of transients.