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.