Hyperpolarization methods offer the possibility of overcoming the inherent sensitivity limits of nuclear magnetic resonance (NMR) given by the thermal Boltzmann spin distribution. The radio-frequency (RF) pulses to monitor the hyperpolarization process alter it by depleting the created magnetization. Possible corrections are simulated with a rate-equation model containing a single source and relaxation rate. The accuracy is demonstrated experimentally, enabling the use of larger flip angles.

A novel cell-free protein synthesis system called eCells produces amino acids based on specific isotopes using low-cost precursors. The system selectively labels methyl groups, i.e valine and leucine, with high efficiency. eCells achieve high levels of ¹³C incorporation and deuteration in protein preparations, making them suitable for NMR experiments of large protein complexes. They are easy to prepare, can be scaled up in volume and are a promising tool for protein production and NMR studies.

We present a tutorial on the cross-polarization experiment, which has been the main method of magnetization transfer in solid-state NMR for decades. We explain the principles of its volume-selective performance in the presence of magic angle spinning and radiofrequency field inhomogeneity and the decrease in efficiency with increasing sample rotation frequency.

Diffusive motion in confined three-site relaxation exchange was studied in Monte Carlo simulations. In thermodynamic equilibrium, the cross-peaks in NMR relaxation exchange maps are symmetric. Asymmetry is observed in mass-balanced driven equilibrium corresponding to circular flow. If this motion can be stimulated by external forces, it can be beneficial to heterogeneous catalysis.

This paper describes the design and implementation of new technology for nuclear magnetic resonance, which is a technique used to understand the molecular structure and dynamics of many systems. The spherical sample container and its apparatus introduced in this paper are used to perform initial proof-of-principle experiments at cryogenic temperatures. Further development of this technology will facilitate more flexibility in magnetic resonance experiments.

We recently liberated the solid effect of dynamic nuclear polarization (DNP) from its perturbative treatment by describing the relevant spin dynamics in a time domain. This allows us to easily account for dynamical processes that modulate the spin interactions in liquids, like the translational diffusion of spins. Here we additionally model the slow rotational diffusion of the polarizing agent and analyze DNP data from nitroxide spin labels in lipid bilayers at 9.4 T.

In nuclear magnetic resonance, the magnetization of abundantly present nuclei contributes to the overall field felt by the same nuclei through intermolecular dipolar interactions. This has led to many surprising discoveries, such as multiple-spin echoes and intermolecular cross-peaks in 2D spectroscopy. In this work, the effect of the dipolar field under continuous irradiation is investigated. Various methods to obtain intermolecular transfer of phase coherences are presented.