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.

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.

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.