Recent  

We introduce the PRESERVE pulse sequence element, allowing variable flip-angle adjustment in 2D ¹H-¹⁵N and ¹H-¹³C 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 through the design and optimization of NMR pulse sequences.

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.

This paper shows the design, simulations and experimental performance of a 35 GHz 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 for 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.

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 made this possible in a time- and effort-efficient manner. 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.