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Updated: Dec 29, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
Heteronuclear cross-relaxation effect modulated by the dynamics of N-functional groups in the solid state under 15N
Heeyong Park1, Boran Uluca-Yazgi2, Saskia Heumann3
1Max Planck Institute for Chemical Energy Conversion, Department of Heterogeneous Reactions, 45470 Mülheim an der Ruhr, Germany; Forschungszentrum Jülich, IEK-9, 52425 Jülich, Germany; RWTH Aachen University, Institute of Technical and Macromolecular Chemistry, 52074 Aachen, Germany.
Abstract:
In a typical magic-angle spinning (MAS) dynamic nuclear polarization (DNP) nuclear magnetic resonance (NMR) experiment, several mechanisms are simultaneously involved when transferring much larger polarization of electron spins to NMR active nuclei of interest. Recently, specific cross-relaxation enhancement by active motions under DNP (SCREAM-DNP) [Daube et al. JACS 2016] has been reported as one of these mechanisms. Thereby 13C enhancement with inverted sign was observed in a direct polarization (DP) MAS DNP experiment, caused by reorientation dynamics of methyl that was not frozen out at 100 K. Here, we report on the spontaneous polarization transfer from hyperpolarized 1H to both primary amine and ammonium nitrogens, resulting in an additional positive signal enhancement in the 15N NMR spectra during 15N DP-MAS DNP. The cross-relaxation induced signal enhancement (CRE) for 15N is of opposite sign compared to that observed for 13C due to the negative sign of the gyromagnetic ratio of 15N. The influence on CRE efficiency caused by variation of the radical solution composition and by temperature was also investigated.
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