Electron spins sense their environment via magnetic interactions. An important contribution stems from nuclear spins in their vicinity. They cause loss of coherence and thus reduce resolution of spectra obtained by experiments on electron spins and the efficiency of transferring electron-spin magentization to other nuclear spins. Here we study how protons in trityl radicals contribute to coherence loss. Such coherence loss is slower in the presence of a strong microwave field.

Electron spin dynamics during microwave irradiation are of increasing interest in electron paramagnetic resonance (EPR) spectroscopy. Here, we show that these dynamics can be probed by modern pulse EPR experiments that use shaped microwave pulses. Combined with spin dynamics simulations, these results provide a starting point for optimizing existing EPR experiments and for developing new pulse sequences.

We believe that, in addition to nontrivial theoretical interest, the proposed work offers experimenters a reliable time interval in which the experimentally measured signal allows a relatively simple interpretation uncomplicated by contributions from three-particle dynamical correlations of having spins nuclei in condensed matter.

Sensitivity is often the limiting factor in ENDOR. Here, we demonstrate how using chirp radiofrequency pulses can improve ENDOR sensitivity up to 3-9-fold, with the strongest increase for broader lines often encountered in disordered solids for nuclei such as nitrogen and metals. The resulting drastic speed-up in acquisition times renders also 2D ENDOR more feasible, as we demonstrate in 2D TRIPLE showing correlations of Cu hyperfine couplings.

The paper investigates the suitability of an existing solution-state NMR spin decoupling sequence for use as a low-power solid-state NMR decoupling sequence under sample spinning. Complications arise from resonance conditions between the spin modulations by the pulse sequence and the sample rotation. We show that the timing of the pulse sequence is the most important criterion to achieve good decoupling. The paper gives recommendations for optimum parameters.

We developed a workflow using FEM simulations to optimize electrochemical NMR (EC-NMR) cell designs by accurately matching B₀ and B₁ field simulations with experimental data. Guidelines for enhanced sensitivity and field homogeneity are given. A B₁ amplification effect in coin cells is described by empirical formula, which has the potential to improve spatial selectivity in future EC-NMR applications.

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.