Zero-Field NMR of Urea: Spin-Topology Engineering by Chemical Exchange

Well-resolved and information-rich J-spectra are the foundation for chemical detection in zero-field NMR. However, even for relatively small molecules, spectra exhibit complexity, hindering the analysis. To address this problem, we investigate an example biomolecule with a complex J-coupling network.urea, a key metabolite in protein catabolism.and demonstrate ways of simplifying its zero-field spectra by modifying spin topology. This goal is achieved by controlling pH-dependent chemical exchange rates of H-1 nuclei and varying the composition of the D2O/H2O mixture used as a solvent. Specifically, we demonstrate that by increasing the proton exchange rate in the [C-13,N-15(2)]-urea solution, the spin system simplifies, manifesting through a single narrow spectral peak. Additionally, we show that the spectra of H-1/D isotopologues of [N-15(2)]-urea can be understood easily by analyzing isolated spin subsystems. This study paves the way for zero-field NMR detection of complex biomolecules, particularly in biofluids with a high concentration of water.

Automated summary

This study investigates an example biomolecule with a complex J-coupling network and demonstrates methods of simplifying zero-field spectra by modifying spin topology. By controlling pH-dependent chemical exchange rates and varying the solvent composition, the goal of achieving a single narrow spectral peak in the spin system is achieved. The study also shows that the spectra of isotopologues can be easily understood by analyzing isolated spin subsystems.