High critical field superconductors are less sensitive to magnet quenching, providing even higher fields. They can be cooled using cryogens like Helium, but simply using an oscillating pressure field. Using solar or wind energy, the cheap cooling promises magnetic resonance at high field, low operating cost, and renewable energy. Such magnets, made compact, can be used to prepolarise chemical samples, to be analysed in benchtop NMR systems, with better nuclear magnetic resonance spectra.

By reviewing attendee lists of ten MR (magnetic resonance) meetings over the last year, we estimate the climate footprint of conferences and explore possibilities to reduce it. This manuscript will facilitate discussions about possible actions the community may take.

In achiral PFAS with 2–3 CF₂ groups, long-lived ¹⁹F spin states (T_LLS) were measured and found to last about 3× longer than T₁ in a static 11.6 T field. These lifetimes are sensitive to macromolecular binding, making them useful for screening fluorinated drugs. T_LLS and T₁ are expected to increase at lower fields where ¹⁹F CSA effects are weaker.

Proteins structure and motion are key to their 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 lifetime using advanced EPR techniques. Our findings show how lifetime can be extended to design better protein analysis.

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

Demonstration of an ultra-compact spectrometer for electrically-detected magnetic resonance on a chip (EDMRoC) of silicon carbide MOSFETs with comparable signal-to-noise ratio as state-of-the-art conventional resonator-based EDMR. The relatively low cost, high sensitivity and limited space requirements of the EDMRoC configuration holds promise for application in basic and applied research as well as in industrial environments.

The magic angle spinning (MAS) technique of solid state NMR requires samples to be rapidly rotated within a magnetic field. The rotation rate speed record is 150 kHz, or 9 million RPM, and hence MAS turbines hold the world rotation speed record for extended objects. The containers holding the samples are made of the strongest materials known, to be able to withstand the excessive centrifugal forces. To overcome the speed limit, this paper delineates a way to do so using an optical tweezers setup

Providing evidence that proteins are dynamical molecules is a major contribution of solution NMR to structural biology. But the classical experiments to measure dynamics can only be applied to small proteins. This is regretful, because larger proteins often display conformational changes in which dynamics plays a functional role. We show here that dynamic information can be extracted from HSQC NMR spectra using a computational approach. Such spectra are widely available also for larger proteins.

We show here that information about protein molecular dynamics can be directly extracted out of a single NMR spectrum. Understanding protein dynamics is essential to understanding its function, energetics and biology. We hope that this contribution helps bring this insight to a much broader application field and audience community than previously possible.

The demonstration of the Finite Pulse Radio Frequency Driven Recoupling experiment was firstly published over the past 20 years. Since it has become one of the used experiments. In this article we consider that experiment using other theoretical and simulated approaches with respect to the previous works. These approaches help us to understand more clearly the influence of each part of that experiment and to see how exactly the spin system is evaluated during it.

We recently added 2D NMR spectroscopy to the well-established techniques able to obtain information on the process of unfolding using resonances of residues in the hydrophobic core of a protein. We asked whether a detailed analysis of the individual stability curves could provide additional site-specific information. By monitoring both cold and heat denaturation of individual residues we convincingly demonstrate that the two unfolding processes are intrinsically different.

Nowadays, almost all MRI technique used in clinical applications are based on a Fourier transformation of the raw data. Alternative non-Fourier magnetic resonance imaging techniques can offer some advantages under certain conditions. SPatio-temporal ENcoding (SPEN) is a non-Fourier method that usually employs frequency-swept radio frequency pulses and can give good images in inhomogeneous magnetic fields. In this work we show how one can improve this technique by using quadratic gradients.