A protein is produced where a single amino acid type is substituted globally by a fluorinated analogue. Through-space fluorine–fluorine contacts are observed by ¹⁹F NMR (nuclear magnetic resonance) spectroscopy. Substitution of methyl groups by CH₂F groups yields outstanding spectral resolution with minimal structural perturbation of the protein. Our work identifies the γ-gauche effect as the main reason for the spectral dispersion.

Nuclear quadrupole resonance is a sensitive technique for studying local structure. However, materials whose local structure is disordered can produce very wide spectra that are both technically challenging and require a lot of human-hours to measure. We present a set-up that acquires these spectra automatically over a wide frequency range. We demonstrate this set-up on several lead halide perovskites at variable temperatures and discuss the details uncovered by high-resolution spectra.

3D-printed sample cells inserted into standard 5 mm NMR (nuclear magnetic resonance) tubes are demonstrated to offer improved sensitivity for biomolecular NMR spectroscopy when the quantity of material is limiting. Using an ellipsoidal shape, magnetic field homogeneity inside the microcell to the first order is insensitive to differences in the magnetic susceptibility of the printer resin and solvent. The sample cells are particularly useful at high ionic strength and at ultrahigh magnetic fields.

Parallel NMR (nuclear magnetic resonance) detection enhances measurement throughput for high-throughput screening. However, local gradients in parallel detectors cause field spillover in adjacent channels, leading to spin dephasing and signal loss. This study introduces a compensation scheme using optimized pulses to mitigate gradient-induced field inhomogeneity through coherence locking. The proposed approach offers an effective solution for NMR probes with parallel, independently switchable gradient coils.

Flavoproteins are essential biomolecules involved in many vital processes. Understanding their reactivity requires study of their intermediate semiquinone form. Using advanced spectroscopy and isotopic labeling, we measured key interactions within this state, uncovering subtle changes in the distribution of electron density. These findings refine our understanding of flavoprotein function and highlight the value of combining experiments and computations for studying complex biological systems.

We present a technology that allows for the direct writing of conductive tracks on cylindrical substrates as receiver coils for magnetic resonance (MR) experiments. The structures are written with high precision, which has two benefits. First, the real structures behave very similarly to the simulated designs, reducing the component variation; second, this allows for the writing of coils apart from the fairly straightforward solenoidal coils, thereby making complex designs available for MR microcoils.

Protein structure and motion are key to its function. Using electron paramagnetic resonance (EPR) methods, it is possible to measure distances between magnetic markers like gadolinium ions grafted on proteins. Such measurements rely on the gadolinium phase memory time, determining how long the signal lasts. We studied how nearby atoms and environmental noise affect signal lifetimes using advanced EPR techniques. Our findings show how lifetimes can be extended to design better protein analysis.

Investigating NMR (nuclear magnetic resonance) phenomena at variable magnetic fields is useful and insightful for hyperpolarization and molecular dynamics in particular. To benefit from high-resolution at high magnetic fields, field-dependent investigations can be performed using a high-field NMR spectrometer, with a sample shuttle apparatus for field cycling. Here, we introduce a new design of a sample shuttle which is fast, reliable, and narrow. We show a series of applications involving small molecules and a protein in solution.