We used NMR to sequentially assign the side-chain resonances of the cytosolic domain of glycoprotein n of the Crimean–Congo hemorrhagic fever virus. The combination of cell-free protein synthesis with high-field NMR and artificial intelligence approaches facilitated a time- and effort-efficient approach. Our results will be harnessed to study the membrane-bound form of the domain and its interactions with virulence factors, which will ultimately help to understand their role in disease.

Scalar couplings give rise to peak splitting in nuclear magnetic resonance (NMR) spectra. Couplings between atoms that span a rotatable bond report on the rotation angle of the bond. Here, we describe a new computational method that can be used to analyze complex patterns of peak splitting. In addition to showing new ways of visualizing and analyzing the underlying data, we uncover how isolated parts of proteins behave differently than when they are embedded in a folded protein.

The nuclear magnetic resonance (NMR) spectroscopy of the ¹⁰³Rh nucleus is onerous owing to its dismal sensitivity. Here, we utilise modern techniques to boost the sensitivity and acquire valuable ¹⁰³Rh NMR parameters for the Rh(acac)₃ transition-metal complex. We acquire proton-enhanced ¹⁰³Rh NMR spectra and successfully characterise the ¹⁰³Rh spin relaxation. In doing so, we unveil the secrets of a complex that is of significant interest to the ¹⁰³Rh NMR and wider chemical community alike.

We introduce the PRESERVE pulse sequence element, allowing variable flip-angle adjustment in 2D ¹H–¹⁵N and ¹H–¹³C transverse-relaxation-optimized-spectroscopy (TROSY)-type correlation experiments. PRESERVE-TROSY exploits a remarkable array of up to nine orthogonal polarization-coherence transfer pathways, showcasing the remarkable potential of spin manipulations achievable via the design and optimization of nuclear magnetic resonance (NMR) pulse sequences.

We show the design, simulations, and experimental performance of a 35 GHz electron paramagnetic resonance (EPR) resonator based on a cylindrical cavity with 3 mm sample access. The design is robust; simple to manufacture and maintain; and, with its elevated Q value, well-suited to sensitive EPR experiments using continuous-wave or low-power pulsed excitation. Thus, we make multi-frequency EPR spectroscopy, a powerful approach to deconvolute overlapping paramagnetic species, more accessible.

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 needed to achieve good decoupling. The paper gives recommendations for optimum parameters.

We developed a workflow using finite element methods to optimise electrochemical cell designs for in operando nuclear magnetic resonance by accurately matching magnetic field and radio frequency field simulations with experimental data. Guidelines for enhanced sensitivity and field homogeneity are given. A radio frequency amplification effect in coin cells is described by empirical formulae, which have the potential to improve spatial selectivity in future in operando applications.